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PDBsum entry 1shg

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protein links
Cytoskeleton PDB id
1shg
Jmol
Contents
Protein chain
57 a.a. *
* Residue conservation analysis
PDB id:
1shg
Name: Cytoskeleton
Title: Crystal structure of a src-homology 3 (sh3) domain
Structure: Alpha-spectrin sh3 domain. Chain: a. Engineered: yes
Source: Gallus gallus. Chicken. Organism_taxid: 9031
Resolution:
1.80Å     R-factor:   0.195     R-free:   0.277
Authors: M.Noble,R.Pauptit,A.Musacchio,M.Saraste,R.K.Wierenga
Key ref: A.Musacchio et al. (1992). Crystal structure of a Src-homology 3 (SH3) domain. Nature, 359, 851-855. PubMed id: 1279434 DOI: 10.1038/359851a0
Date:
19-May-93     Release date:   31-Oct-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07751  (SPTA2_CHICK) -  Spectrin alpha chain, non-erythrocytic 1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2477 a.a.
57 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     endocytosis   1 term 

 

 
DOI no: 10.1038/359851a0 Nature 359:851-855 (1992)
PubMed id: 1279434  
 
 
Crystal structure of a Src-homology 3 (SH3) domain.
A.Musacchio, M.Noble, R.Pauptit, R.Wierenga, M.Saraste.
 
  ABSTRACT  
 
The Src-homologous SH3 domain is a small domain present in a large number of proteins that are involved in signal transduction, such as the Src protein tyrosine kinase, or in membrane-cytoskeleton interactions, but the function of SH3 is still unknown (reviewed in refs 1-3). Here we report the three-dimensional structure at 1.8 A resolution of the SH3 domain of the cytoskeletal protein spectrin expressed in Escherichia coli. The domain is a compact beta-barrel made of five antiparallel beta-strands. The amino acids that are conserved in the SH3 sequences are located close to each other on one side of the molecule. This surface is rich in aromatic and carboxylic amino acids, and is distal to the region of the molecule where the N and C termini reside and where SH3 inserts into the alpha-spectrin chain. We suggest that a protein ligand binds to this conserved surface of SH3.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20668894 A.J.Baines (2010).
The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life.
  Protoplasma, 244, 99.  
19882298 M.Carducci, L.Licata, D.Peluso, L.Castagnoli, and G.Cesareni (2010).
Enriching the viral-host interactomes with interactions mediated by SH3 domains.
  Amino Acids, 38, 1541-1547.  
20467438 M.I.Arbuckle, N.H.Komiyama, A.Delaney, M.Coba, E.M.Garry, R.Rosie, A.J.Allchorne, L.H.Forsyth, M.Bence, H.J.Carlisle, T.J.O'Dell, R.Mitchell, S.M.Fleetwood-Walker, and S.G.Grant (2010).
The SH3 domain of postsynaptic density 95 mediates inflammatory pain through phosphatidylinositol-3-kinase recruitment.
  EMBO Rep, 11, 473-478.  
21209864 S.Azzi, V.Parissi, R.G.Maroun, P.Eid, O.Mauffret, and S.Fermandjian (2010).
The HIV-1 integrase α4-helix involved in LTR-DNA recognition is also a highly antigenic peptide element.
  PLoS One, 5, e16001.  
19937113 Z.Hobaika, L.Zargarian, R.G.Maroun, O.Mauffret, T.R.Burke, and S.Fermandjian (2010).
HIV-1 integrase and virus and cell DNAs: complex formation and perturbation by inhibitors of integration.
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19966410 A.Cámara-Artigas, M.Andújar-Sánchez, E.Ortiz-Salmerón, C.Cuadri, and S.Casares (2009).
The effect of a proline residue on the rate of growth and the space group of alpha-spectrin SH3-domain crystals.
  Acta Crystallogr D Biol Crystallogr, 65, 1247-1252.
PDB code: 3i9q
19141864 J.J.Ipsaro, L.Huang, and A.Mondragón (2009).
Structures of the spectrin-ankyrin interaction binding domains.
  Blood, 113, 5385-5393.
PDB codes: 3f57 3f59
19582374 J.Xu, Y.Xue, and N.R.Skrynnikov (2009).
Detection of nanosecond time scale side-chain jumps in a protein dissolved in water/glycerol solvent.
  J Biomol NMR, 45, 57-72.  
19168783 P.R.Stabach, I.Simonović, M.A.Ranieri, M.S.Aboodi, T.A.Steitz, M.Simonovi, and J.S.Morrow (2009).
The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties.
  Blood, 113, 5377-5384.
PDB code: 3edu
19432457 S.P.Edmondson, J.Turri, K.Smith, A.Clark, and J.W.Shriver (2009).
Structure, stability, and flexibility of ribosomal protein L14e from Sulfolobus solfataricus.
  Biochemistry, 48, 5553-5562.  
  20457566 V.Bennett, and J.Healy (2009).
Membrane domains based on ankyrin and spectrin associated with cell-cell interactions.
  Cold Spring Harb Perspect Biol, 1, a003012.  
19808934 Z.Hobaika, L.Zargarian, Y.Boulard, R.G.Maroun, O.Mauffret, and S.Fermandjian (2009).
Specificity of LTR DNA recognition by a peptide mimicking the HIV-1 integrase {alpha}4 helix.
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18045873 A.Rutkowska, M.P.Mayer, A.Hoffmann, F.Merz, B.Zachmann-Brand, C.Schaffitzel, N.Ban, E.Deuerling, and B.Bukau (2008).
Dynamics of trigger factor interaction with translating ribosomes.
  J Biol Chem, 283, 4124-4132.  
19081052 P.Robustelli, A.Cavalli, and M.Vendruscolo (2008).
Determination of protein structures in the solid state from NMR chemical shifts.
  Structure, 16, 1764-1769.
PDB code: 2k0p
17164526 J.Gruber, A.Zawaira, R.Saunders, C.P.Barrett, and M.E.Noble (2007).
Computational analyses of the surface properties of protein-protein interfaces.
  Acta Crystallogr D Biol Crystallogr, 63, 50-57.  
17010654 N.Dimasi (2007).
Crystal structure of the C-terminal SH3 domain of the adaptor protein GADS in complex with SLP-76 motif peptide reveals a unique SH3-SH3 interaction.
  Int J Biochem Cell Biol, 39, 109-123.
PDB code: 2d0n
17189480 Q.Wang, M.A.Deloia, Y.Kang, C.Litchke, N.Zhang, M.A.Titus, and K.J.Walters (2007).
The SH3 domain of a M7 interacts with its C-terminal proline-rich region.
  Protein Sci, 16, 189-196.
PDB code: 2i0n
17407569 S.Casares, E.Ab, H.Eshuis, O.Lopez-Mayorga, N.A.van Nuland, and F.Conejero-Lara (2007).
The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: understanding the determinants of binding affinity by comparison with Abl-SH3.
  BMC Struct Biol, 7, 22.
PDB codes: 2jm8 2jm9 2jma
17330285 S.Casares, O.López-Mayorga, M.C.Vega, A.Cámara-Artigas, and F.Conejero-Lara (2007).
Cooperative propagation of local stability changes from low-stability and high-stability regions in a SH3 domain.
  Proteins, 67, 531-547.
PDB codes: 2cdt 2f2v 2f2w 2f2x
17597155 S.Lowey, L.D.Saraswat, H.Liu, N.Volkmann, and D.Hanein (2007).
Evidence for an interaction between the SH3 domain and the N-terminal extension of the essential light chain in class II myosins.
  J Mol Biol, 371, 902-913.  
17389688 Y.Li, N.Clough, X.Sun, W.Yu, B.L.Abbott, C.J.Hogan, and Z.Dai (2007).
Bcr-Abl induces abnormal cytoskeleton remodeling, beta1 integrin clustering and increased cell adhesion to fibronectin through the Abl interactor 1 pathway.
  J Cell Sci, 120, 1436-1446.  
16407311 A.Hoffmann, F.Merz, A.Rutkowska, B.Zachmann-Brand, E.Deuerling, and B.Bukau (2006).
Trigger factor forms a protective shield for nascent polypeptides at the ribosome.
  J Biol Chem, 281, 6539-6545.  
16718600 M.L.Cartron, S.Maddocks, P.Gillingham, C.J.Craven, and S.C.Andrews (2006).
Feo--transport of ferrous iron into bacteria.
  Biometals, 19, 143-157.  
16263932 A.Esteras-Chopo, L.Serrano, and M.López de la Paz (2005).
The amyloid stretch hypothesis: recruiting proteins toward the dark side.
  Proc Natl Acad Sci U S A, 102, 16672-16677.  
15657040 C.Massenet, S.Chenavas, C.Cohen-Addad, M.C.Dagher, G.Brandolin, E.Pebay-Peyroula, and F.Fieschi (2005).
Effects of p47phox C terminus phosphorylations on binding interactions with p40phox and p67phox. Structural and functional comparison of p40phox and p67phox SH3 domains.
  J Biol Chem, 280, 13752-13761.
PDB codes: 1w6x 1w70
16175529 M.Fossi, F.Castellani, M.Nilges, H.Oschkinat, and B.J.van Rossum (2005).
SOLARIA: a protocol for automated cross-peak assignment and structure calculation for solid-state magic-angle spinning NMR spectroscopy.
  Angew Chem Int Ed Engl, 44, 6151-6154.  
15928996 V.Chevelkov, K.Faelber, A.Diehl, U.Heinemann, H.Oschkinat, and B.Reif (2005).
Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR.
  J Biomol NMR, 31, 295-310.
PDB code: 1u06
14978284 A.M.Fernández-Escamilla, M.S.Cheung, M.C.Vega, M.Wilmanns, J.N.Onuchic, and L.Serrano (2004).
Solvation in protein folding analysis: combination of theoretical and experimental approaches.
  Proc Natl Acad Sci U S A, 101, 2834-2839.
PDB code: 1uue
14747656 R.I.MacDonald, and J.A.Cummings (2004).
Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer.
  Proc Natl Acad Sci U S A, 101, 1502-1507.  
12660159 G.Skiniotis, T.Surrey, S.Altmann, H.Gross, Y.H.Song, E.Mandelkow, and A.Hoenger (2003).
Nucleotide-induced conformations in the neck region of dimeric kinesin.
  EMBO J, 22, 1518-1528.  
12945054 H.Fan, and A.E.Mark (2003).
Relative stability of protein structures determined by X-ray crystallography or NMR spectroscopy: a molecular dynamics simulation study.
  Proteins, 53, 111-120.  
12837782 J.A.D'Aquino, and D.Ringe (2003).
Determinants of the SRC homology domain 3-like fold.
  J Bacteriol, 185, 4081-4086.
PDB code: 1p92
12824493 L.Spagnolo, S.Ventura, and L.Serrano (2003).
Folding specificity induced by loop stiffness.
  Protein Sci, 12, 1473-1482.  
12620234 Q.Liu, D.Berry, P.Nash, T.Pawson, C.J.McGlade, and S.S.Li (2003).
Structural basis for specific binding of the Gads SH3 domain to an RxxK motif-containing SLP-76 peptide: a novel mode of peptide recognition.
  Mol Cell, 11, 471-481.
PDB code: 1h3h
11854494 A.Liwo, P.Arłukowicz, C.Czaplewski, S.Ołdziej, J.Pillardy, and H.A.Scheraga (2002).
A method for optimizing potential-energy functions by a hierarchical design of the potential-energy landscape: application to the UNRES force field.
  Proc Natl Acad Sci U S A, 99, 1937-1942.  
11959988 A.R.Viguera, C.Vega, and L.Serrano (2002).
Unspecific hydrophobic stabilization of folding transition states.
  Proc Natl Acad Sci U S A, 99, 5349-5354.
PDB code: 1hd3
12422222 F.Castellani, B.van Rossum, A.Diehl, M.Schubert, K.Rehbein, and H.Oschkinat (2002).
Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy.
  Nature, 420, 98.
PDB code: 1m8m
12138090 H.S.Oh, H.Kwon, S.K.Sun, and C.H.Yang (2002).
QM, a putative tumor suppressor, regulates proto-oncogene c-yes.
  J Biol Chem, 277, 36489-36498.  
11805324 M.S.Cheung, A.E.García, and J.N.Onuchic (2002).
Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapse.
  Proc Natl Acad Sci U S A, 99, 685-690.  
12006985 S.Ventura, M.C.Vega, E.Lacroix, I.Angrand, L.Spagnolo, and L.Serrano (2002).
Conformational strain in the hydrophobic core and its implications for protein folding and design.
  Nat Struct Biol, 9, 485-493.
PDB codes: 1e6g 1e6h 1h8k
11948879 B.J.van Rossum, F.Castellani, K.Rehbein, J.Pauli, and H.Oschkinat (2001).
Assignment of the nonexchanging protons of the alpha-spectrin SH3 domain by two- and three-dimensional 1H-13C solid-state magic-angle spinning NMR and comparison of solution and solid-state proton chemical shifts.
  Chembiochem, 2, 906-914.  
11682324 M.Vidal, V.Gigoux, and C.Garbay (2001).
SH2 and SH3 domains as targets for anti-proliferative agents.
  Crit Rev Oncol Hematol, 40, 175-186.  
11173498 R.Berisio, A.Viguera, L.Serrano, and M.Wilmanns (2001).
Atomic resolution structure of a mutant of the spectrin SH3 domain.
  Acta Crystallogr D Biol Crystallogr, 57, 337-340.
PDB code: 1g2b
10856234 H.Kang, C.Freund, J.S.Duke-Cohan, A.Musacchio, G.Wagner, and C.E.Rudd (2000).
SH3 domain recognition of a proline-independent tyrosine-based RKxxYxxY motif in immune cell adaptor SKAP55.
  EMBO J, 19, 2889-2899.  
10869177 J.A.Bousquet, C.Garbay, B.P.Roques, and Y.Mély (2000).
Circular dichroic investigation of the native and non-native conformational states of the growth factor receptor-binding protein 2 N-terminal src homology domain 3: effect of binding to a proline-rich peptide from guanine nucleotide exchange factor.
  Biochemistry, 39, 7722-7735.  
  10892804 K.Raha, A.M.Wollacott, M.J.Italia, and J.R.Desjarlais (2000).
Prediction of amino acid sequence from structure.
  Protein Sci, 9, 1106-1119.  
  11206053 M.C.Vega, J.C.Martínez, and L.Serrano (2000).
Thermodynamic and structural characterization of Asn and Ala residues in the disallowed II' region of the Ramachandran plot.
  Protein Sci, 9, 2322-2328.
PDB codes: 1qkw 1qkx
10467125 B.Aghazadeh, and M.K.Rosen (1999).
Ligand recognition by SH3 and WW domains: the role of N-alkylation in PPII helices.
  Chem Biol, 6, R241-R246.  
10025403 C.Kambach, S.Walke, R.Young, J.M.Avis, E.de la Fortelle, V.A.Raker, R.Lührmann, J.Li, and K.Nagai (1999).
Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs.
  Cell, 96, 375-387.
PDB codes: 1b34 1d3b
9888794 J.C.Martínez, A.R.Viguera, R.Berisio, M.Wilmanns, P.L.Mateo, V.V.Filimonov, and L.Serrano (1999).
Thermodynamic analysis of alpha-spectrin SH3 and two of its circular permutants with different loop lengths: discerning the reasons for rapid folding in proteins.
  Biochemistry, 38, 549-559.
PDB code: 1pwt
  10388809 K.Colwill, D.Field, L.Moore, J.Friesen, and B.Andrews (1999).
In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions.
  Genetics, 152, 881-893.  
10413463 M.Sadqi, S.Casares, M.A.Abril, O.López-Mayorga, F.Conejero-Lara, and E.Freire (1999).
The native state conformational ensemble of the SH3 domain from alpha-spectrin.
  Biochemistry, 38, 8899-8906.  
9631289 A.McGough (1998).
F-actin-binding proteins.
  Curr Opin Struct Biol, 8, 166-176.  
9665171 C.A.Bewley, K.R.Gustafson, M.R.Boyd, D.G.Covell, A.Bax, G.M.Clore, and A.M.Gronenborn (1998).
Solution structure of cyanovirin-N, a potent HIV-inactivating protein.
  Nat Struct Biol, 5, 571-578.
PDB codes: 2ezm 2ezn
9736607 D.J.Owen, P.Wigge, Y.Vallis, J.D.Moore, P.R.Evans, and H.T.McMahon (1998).
Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation.
  EMBO J, 17, 5273-5285.
PDB code: 1bb9
9593709 D.Ziemnicka-Kotula, J.Xu, H.Gu, A.Potempska, K.S.Kim, E.C.Jenkins, E.Trenkner, and L.Kotula (1998).
Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton.
  J Biol Chem, 273, 13681-13692.  
9565752 E.Lacroix, A.R.Viguera, and L.Serrano (1998).
Reading protein sequences backwards.
  Fold Des, 3, 79-85.  
9699637 J.C.Martinez, M.T.Pisabarro, and L.Serrano (1998).
Obligatory steps in protein folding and the conformational diversity of the transition state.
  Nat Struct Biol, 5, 721-729.
PDB code: 1bk2
9819209 K.L.Maxwell, and A.R.Davidson (1998).
Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects.
  Biochemistry, 37, 16172-16182.  
9694876 K.Okkenhaug, and R.Rottapel (1998).
Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain-proline interaction.
  J Biol Chem, 273, 21194-21202.  
9485402 K.W.Plaxco, J.I.Guijarro, C.J.Morton, M.Pitkeathly, I.D.Campbell, and C.M.Dobson (1998).
The folding kinetics and thermodynamics of the Fyn-SH3 domain.
  Biochemistry, 37, 2529-2537.  
9741847 L.Holm, and C.Sander (1998).
Dictionary of recurrent domains in protein structures.
  Proteins, 33, 88-96.  
9632734 M.Majidi, A.E.Hubbs, and J.H.Lichy (1998).
Activation of extracellular signal-regulated kinase 2 by a novel Abl-binding protein, ST5.
  J Biol Chem, 273, 16608-16614.  
9593201 S.Knapp, P.T.Mattson, P.Christova, K.D.Berndt, A.Karshikoff, M.Vihinen, C.I.Smith, and R.Ladenstein (1998).
Thermal unfolding of small proteins with SH3 domain folding pattern.
  Proteins, 31, 309-319.  
9360611 A.R.Viguera, and L.Serrano (1997).
Loop length, intramolecular diffusion and protein folding.
  Nat Struct Biol, 4, 939-946.  
9329088 B.L.de Groot, D.M.van Aalten, R.M.Scheek, A.Amadei, G.Vriend, and H.J.Berendsen (1997).
Prediction of protein conformational freedom from distance constraints.
  Proteins, 29, 240-251.  
9566119 D.C.Dalgarno, M.C.Botfield, and R.J.Rickles (1997).
SH3 domains and drug design: ligands, structure, and biological function.
  Biopolymers, 43, 383-400.  
9408950 H.V.Patel, S.R.Tzeng, C.Y.Liao, S.H.Chen, and J.W.Cheng (1997).
SH3 domain of Bruton's tyrosine kinase can bind to proline-rich peptides of TH domain of the kinase and p120cbl.
  Proteins, 29, 545-552.  
9241420 J.Kuriyan, and D.Cowburn (1997).
Modular peptide recognition domains in eukaryotic signaling.
  Annu Rev Biophys Biomol Struct, 26, 259-288.  
9287337 J.Meriläinen, V.P.Lehto, and V.M.Wasenius (1997).
FAP52, a novel, SH3 domain-containing focal adhesion protein.
  J Biol Chem, 272, 23278-23284.  
9034330 K.Q.Hu, and J.Settleman (1997).
Tandem SH2 binding sites mediate the RasGAP-RhoGAP interaction: a conformational mechanism for SH3 domain regulation.
  EMBO J, 16, 473-483.  
9303002 K.V.Kishan, G.Scita, W.T.Wong, P.P.Di Fiore, and M.E.Newcomer (1997).
The SH3 domain of Eps8 exists as a novel intertwined dimer.
  Nat Struct Biol, 4, 739-743.
PDB code: 1aoj
9278444 M.Y.Kanemitsu, L.W.Loo, S.Simon, A.F.Lau, and W.Eckhart (1997).
Tyrosine phosphorylation of connexin 43 by v-Src is mediated by SH2 and SH3 domain interactions.
  J Biol Chem, 272, 22824-22831.  
9150946 R.K.Rasmussen, H.Ji, J.S.Eddes, R.L.Moritz, G.E.Reid, R.J.Simpson, and D.S.Dorow (1997).
Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2.
  Electrophoresis, 18, 588-598.  
8836105 A.R.Viguera, L.Serrano, and M.Wilmanns (1996).
Different folding transition states may result in the same native structure.
  Nat Struct Biol, 3, 874-880.  
8805554 C.J.Morton, D.J.Pugh, E.L.Brown, J.D.Kahmann, D.A.Renzoni, and I.D.Campbell (1996).
Solution structure and peptide binding of the SH3 domain from human Fyn.
  Structure, 4, 705-714.
PDB codes: 1nyf 1nyg
  8605874 D.C.Chan, M.T.Bedford, and P.Leder (1996).
Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains.
  EMBO J, 15, 1045-1054.  
8789085 D.M.van Aalten, A.Amadei, R.Bywater, J.B.Findlay, H.J.Berendsen, C.Sander, and P.F.Stouten (1996).
A comparison of structural and dynamic properties of different simulation methods applied to SH3.
  Biophys J, 70, 684-692.  
8805596 H.J.Nam, W.G.Haser, T.M.Roberts, and C.A.Frederick (1996).
Intramolecular interactions of the regulatory domains of the Bcr-Abl kinase reveal a novel control mechanism.
  Structure, 4, 1105-1114.
PDB code: 2abl
8626778 K.Wang, M.Knipfer, Q.Q.Huang, A.van Heerden, L.C.Hsu, G.Gutierrez, X.L.Quian, and H.Stedman (1996).
Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3.
  J Biol Chem, 271, 4304-4314.  
8718852 M.T.Pisabarro, and L.Serrano (1996).
Rational design of specific high-affinity peptide ligands for the Abl-SH3 domain.
  Biochemistry, 35, 10634-10640.  
8696976 P.Rice, R.Craigie, and D.R.Davies (1996).
Retroviral integrases and their cousins.
  Curr Opin Struct Biol, 6, 76-83.  
  9116759 S.J.McClure, and P.J.Robinson (1996).
Dynamin, endocytosis and intracellular signalling (review).
  Mol Membr Biol, 13, 189-215.  
8663328 T.Erpel, G.Alonso, S.Roche, and S.A.Courtneidge (1996).
The Src SH3 domain is required for DNA synthesis induced by platelet-derived growth factor and epidermal growth factor.
  J Biol Chem, 271, 16807-16812.  
7552753 A.P.Eijkelenboom, R.A.Lutzke, R.Boelens, R.H.Plasterk, R.Kaptein, and K.Hård (1995).
The DNA-binding domain of HIV-1 integrase has an SH3-like fold.
  Nat Struct Biol, 2, 807-810.  
7719850 D.C.Amberg, E.Basart, and D.Botstein (1995).
Defining protein interactions with yeast actin in vivo.
  Nat Struct Biol, 2, 28-35.  
8536694 D.S.Dorow, L.Devereux, G.F.Tu, G.Price, J.K.Nicholl, G.R.Sutherland, and R.J.Simpson (1995).
Complete nucleotide sequence, expression, and chromosomal localisation of human mixed-lineage kinase 2.
  Eur J Biochem, 234, 492-500.  
  7823917 E.Lam (1995).
Domain analysis of the plant DNA-binding protein GT1a: requirement of four putative alpha-helices for DNA binding and identification of a novel oligomerization region.
  Mol Cell Biol, 15, 1014-1020.  
  7708014 E.M.Phizicky, and S.Fields (1995).
Protein-protein interactions: methods for detection and analysis.
  Microbiol Rev, 59, 94.  
7613864 G.A.Leonard, S.Zhang, M.R.Peterson, S.J.Harrop, J.R.Helliwell, W.B.Cruse, B.L.d'Estaintot, O.Kennard, T.Brown, and W.N.Hunter (1995).
Self-association of a DNA loop creates a quadruplex: crystal structure of d(GCATGCT) at 1.8 A resolution.
  Structure, 3, 335-340.
PDB code: 184d
7755981 H.Q.Sun, K.Kwiatkowska, and H.L.Yin (1995).
Actin monomer binding proteins.
  Curr Opin Cell Biol, 7, 102-110.  
7629118 H.Voliovitch, D.G.Schindler, Y.R.Hadari, S.I.Taylor, D.Accili, and Y.Zick (1995).
Tyrosine phosphorylation of insulin receptor substrate-1 in vivo depends upon the presence of its pleckstrin homology region.
  J Biol Chem, 270, 18083-18087.  
9383403 J.A.Simon, and S.L.Schreiber (1995).
Grb2 SH3 binding to peptides from Sos: evaluation of a general model for SH3-ligand interactions.
  Chem Biol, 2, 53-60.  
7553130 J.M.Robinson, and J.A.Badwey (1995).
The NADPH oxidase complex of phagocytic leukocytes: a biochemical and cytochemical view.
  Histochem Cell Biol, 103, 163-180.  
7536925 K.Alexandropoulos, G.Cheng, and D.Baltimore (1995).
Proline-rich sequences that bind to Src homology 3 domains with individual specificities.
  Proc Natl Acad Sci U S A, 92, 3110-3114.  
9383454 K.M.Shokat (1995).
Tyrosine kinases: modular signaling enzymes with tunable specificities.
  Chem Biol, 2, 509-514.  
7782338 M.Sudol, P.Bork, A.Einbond, K.Kastury, T.Druck, M.Negrini, K.Huebner, and D.Lehman (1995).
Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain.
  J Biol Chem, 270, 14733-14741.  
7598957 S.A.Benner (1995).
Predicting the conformation of proteins from sequences. Progress and future progress.
  J Mol Recognit, 8, 9.  
8618911 S.Feng, C.Kasahara, R.J.Rickles, and S.L.Schreiber (1995).
Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands.
  Proc Natl Acad Sci U S A, 92, 12408-12415.
PDB codes: 1qwe 1qwf
7629101 S.S.Bryant, S.Briggs, T.E.Smithgall, G.A.Martin, F.McCormick, J.H.Chang, S.J.Parsons, and R.Jove (1995).
Two SH2 domains of p120 Ras GTPase-activating protein bind synergistically to tyrosine phosphorylated p190 Rho GTPase-activating protein.
  J Biol Chem, 270, 17947-17952.  
  7534229 T.Erpel, G.Superti-Furga, and S.A.Courtneidge (1995).
Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactions.
  EMBO J, 14, 963-975.  
7657668 W.Yang, S.N.Malek, and S.Desiderio (1995).
An SH3-binding site conserved in Bruton's tyrosine kinase and related tyrosine kinases mediates specific protein interactions in vitro and in vivo.
  J Biol Chem, 270, 20832-20840.  
7735837 X.Wu, B.Knudsen, S.M.Feller, J.Zheng, A.Sali, D.Cowburn, H.Hanafusa, and J.Kuriyan (1995).
Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk.
  Structure, 3, 215-226.
PDB codes: 1cka 1ckb
8590002 Y.Q.Gosser, J.Zheng, M.Overduin, B.J.Mayer, and D.Cowburn (1995).
The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct.
  Structure, 3, 1075-1086.
PDB code: 1awo
7664083 A.Musacchio, M.Saraste, and M.Wilmanns (1994).
High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.
  Nat Struct Biol, 1, 546-551.
PDB codes: 1abo 1abq 1fyn
7953536 C.J.Morton, and I.D.Campbell (1994).
SH3 domains. Molecular 'Velcro'.
  Curr Biol, 4, 615-617.  
7664069 D.Cowburn (1994).
Helical encounter.
  Nat Struct Biol, 1, 489-491.  
  7521298 D.Cussac, M.Frech, and P.Chardin (1994).
Binding of the Grb2 SH2 domain to phosphotyrosine motifs does not change the affinity of its SH3 domains for Sos proline-rich motifs.
  EMBO J, 13, 4011-4021.  
7881903 D.Kohda, H.Terasawa, S.Ichikawa, K.Ogura, H.Hatanaka, V.Mandiyan, A.Ullrich, J.Schlessinger, and F.Inagaki (1994).
Solution structure and ligand-binding site of the carboxy-terminal SH3 domain of GRB2.
  Structure, 2, 1029-1040.
PDB codes: 1gfc 1gfd
  11725009 D.Liu, and L.H.Wang (1994).
Oncogenes, Protein Tyrosine Kinases, and Signal Transduction.
  J Biomed Sci, 1, 65-82.  
8024815 G.L.Johnson, and R.R.Vaillancourt (1994).
Sequential protein kinase reactions controlling cell growth and differentiation.
  Curr Opin Cell Biol, 6, 230-238.  
  7520528 G.Panchamoorthy, T.Fukazawa, L.Stolz, G.Payne, K.Reedquist, S.Shoelson, Z.Songyang, L.Cantley, C.Walsh, and H.Band (1994).
Physical and functional interactions between SH2 and SH3 domains of the Src family protein tyrosine kinase p59fyn.
  Mol Cell Biol, 14, 6372-6385.  
7634092 H.Baumann, S.Knapp, T.Lundbäck, R.Ladenstein, and T.Härd (1994).
Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus.
  Nat Struct Biol, 1, 808-819.
PDB code: 1sso
7773778 H.Terasawa, D.Kohda, H.Hatanaka, S.Tsuchiya, K.Ogura, K.Nagata, S.Ishii, V.Mandiyan, A.Ullrich, and J.Schlessinger (1994).
Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos.
  Nat Struct Biol, 1, 891-897.  
7545075 H.Yu, and S.L.Schreiber (1994).
Signalling an interest.
  Nat Struct Biol, 1, 417-420.  
7984417 J.D.Thompson, D.G.Higgins, and T.J.Gibson (1994).
CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice.
  Nucleic Acids Res, 22, 4673-4680.  
8193536 J.Schlessinger (1994).
SH2/SH3 signaling proteins.
  Curr Opin Genet Dev, 4, 25-30.  
8167031 M.D.Rozycki, J.C.Myslik, C.E.Schutt, and U.Lindberg (1994).
Structural aspects of actin-binding proteins.
  Curr Opin Cell Biol, 6, 87-95.  
7773767 M.Saraste, and A.Musacchio (1994).
Backwards and forwards binding.
  Nat Struct Biol, 1, 835-837.  
7773779 N.Goudreau, F.Cornille, M.Duchesne, F.Parker, B.Tocqué, C.Garbay, and B.P.Roques (1994).
NMR structure of the N-terminal SH3 domain of GRB2 and its complex with a proline-rich peptide from Sos.
  Nat Struct Biol, 1, 898-907.  
7519238 Q.Zhu, M.Zhang, D.J.Rawlings, M.Vihinen, T.Hagemann, D.C.Saffran, S.P.Kwan, L.Nilsson, C.I.Smith, O.N.Witte, S.H.Chen, and H.D.Ochs (1994).
Deletion within the Src homology domain 3 of Bruton's tyrosine kinase resulting in X-linked agammaglobulinemia (XLA).
  J Exp Med, 180, 461-470.  
  7969134 R.R.Mattingly, A.Sorisky, M.R.Brann, and I.G.Macara (1994).
Muscarinic receptors transform NIH 3T3 cells through a Ras-dependent signalling pathway inhibited by the Ras-GTPase-activating protein SH3 domain.
  Mol Cell Biol, 14, 7943-7952.  
7656049 W.A.Lim, and F.M.Richards (1994).
Critical residues in an SH3 domain from Sem-5 suggest a mechanism for proline-rich peptide recognition.
  Nat Struct Biol, 1, 221-225.  
  7987221 W.A.Lim, R.O.Fox, and F.M.Richards (1994).
Stability and peptide binding affinity of an SH3 domain from the Caenorhabditis elegans signaling protein Sem-5.
  Protein Sci, 3, 1261-1266.  
  8137811 Y.S.Yang, C.Garbay, M.Duchesne, F.Cornille, N.Jullian, N.Fromage, B.Tocque, and B.P.Roques (1994).
Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence.
  EMBO J, 13, 1270-1279.  
8236453 A.Musacchio, T.Gibson, P.Rice, J.Thompson, and M.Saraste (1993).
The PH domain: a common piece in the structural patchwork of signalling proteins.
  Trends Biochem Sci, 18, 343-348.  
8210313 A.T.Brünger, and M.Nilges (1993).
Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMR-spectroscopy.
  Q Rev Biophys, 26, 49.  
8493721 B.Rost, R.Schneider, and C.Sander (1993).
Progress in protein structure prediction?
  Trends Biochem Sci, 18, 120-123.  
8357828 C.E.Rudd, O.Janssen, K.V.Prasad, M.Raab, A.da Silva, J.C.Telfer, and M.Yamamoto (1993).
src-related protein tyrosine kinases and their surface receptors.
  Biochim Biophys Acta, 1155, 239-266.  
  8395016 C.M.Pleiman, M.R.Clark, L.K.Gauen, S.Winitz, K.M.Coggeshall, G.L.Johnson, A.S.Shaw, and J.C.Cambier (1993).
Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase.
  Mol Cell Biol, 13, 5877-5887.  
  8453370 C.M.Stultz, J.V.White, and T.F.Smith (1993).
Structural analysis based on state-space modeling.
  Protein Sci, 2, 305-314.  
8335689 D.A.Holtzman, S.Yang, and D.G.Drubin (1993).
Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae.
  J Cell Biol, 122, 635-644.  
7684655 G.W.Booker, I.Gout, A.K.Downing, P.C.Driscoll, J.Boyd, M.D.Waterfield, and I.D.Campbell (1993).
Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase.
  Cell, 73, 813-822.
PDB codes: 1pnj 2pni
8402898 I.Gout, R.Dhand, I.D.Hiles, M.J.Fry, G.Panayotou, P.Das, O.Truong, N.F.Totty, J.Hsuan, and G.W.Booker (1993).
The GTPase dynamin binds to and is activated by a subset of SH3 domains.
  Cell, 75, 25-36.  
  7505680 J.Bajorath, R.Stenkamp, and A.Aruffo (1993).
Knowledge-based model building of proteins: concepts and examples.
  Protein Sci, 2, 1798-1810.
PDB code: 1kjd
8349299 J.C.Cambier, W.Bedzyk, K.Campbell, N.Chien, J.Friedrich, A.Harwood, W.Jensen, C.Pleiman, and M.R.Clark (1993).
The B-cell antigen receptor: structure and function of primary, secondary, tertiary and quaternary components.
  Immunol Rev, 132, 85.  
8394019 K.V.Prasad, O.Janssen, R.Kapeller, M.Raab, L.C.Cantley, and C.E.Rudd (1993).
Src-homology 3 domain of protein kinase p59fyn mediates binding to phosphatidylinositol 3-kinase in T cells.
  Proc Natl Acad Sci U S A, 90, 7366-7370.  
  8246987 K.V.Prasad, R.Kapeller, O.Janssen, H.Repke, J.S.Duke-Cohan, L.C.Cantley, and C.E.Rudd (1993).
Phosphatidylinositol (PI) 3-kinase and PI 4-kinase binding to the CD4-p56lck complex: the p56lck SH3 domain binds to PI 3-kinase but not PI 4-kinase.
  Mol Cell Biol, 13, 7708-7717.  
  7687536 M.E.Noble, A.Musacchio, M.Saraste, S.A.Courtneidge, and R.K.Wierenga (1993).
Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin.
  EMBO J, 12, 2617-2624.
PDB code: 1shf
  8268793 M.J.Fry, G.Panayotou, G.W.Booker, and M.D.Waterfield (1993).
New insights into protein-tyrosine kinase receptor signaling complexes.
  Protein Sci, 2, 1785-1797.  
  7687742 R.B.Birge, J.E.Fajardo, C.Reichman, S.E.Shoelson, Z.Songyang, L.C.Cantley, and H.Hanafusa (1993).
Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts.
  Mol Cell Biol, 13, 4648-4656.  
  8321240 S.Tanaka, S.Hattori, T.Kurata, K.Nagashima, Y.Fukui, S.Nakamura, and M.Matsuda (1993).
Both the SH2 and SH3 domains of human CRK protein are required for neuronal differentiation of PC12 cells.
  Mol Cell Biol, 13, 4409-4415.  
15335710 T.Pawson, and J.Schlessingert (1993).
SH2 and SH3 domains.
  Curr Biol, 3, 434-442.  
  7689147 X.Liu, L.E.Marengere, C.A.Koch, and T.Pawson (1993).
The v-Src SH3 domain binds phosphatidylinositol 3'-kinase.
  Mol Cell Biol, 13, 5225-5232.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.