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PDBsum entry 1h92

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protein links
Transferase PDB id
1h92
Jmol
Contents
Protein chain
63 a.a. *
* Residue conservation analysis
PDB id:
1h92
Name: Transferase
Title: Sh3 domain of human lck tyrosine kinase
Structure: Proto-oncogene tyrosine-protein kinase lck. Chain: a. Fragment: sh3 domain residues 57-119. Synonym: tyrosine-protein kinase lck, p56-lck. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: intracellular. Expressed in: escherichia coli. Expression_system_taxid: 511693.
NMR struc: 30 models
Authors: K.Schweimer,S.Hoffmann,U.Friedrich,B.Biesinger,P.Roesch, H.Sticht
Key ref:
K.Schweimer et al. (2002). Structural investigation of the binding of a herpesviral protein to the SH3 domain of tyrosine kinase Lck. Biochemistry, 41, 5120-5130. PubMed id: 11955060 DOI: 10.1021/bi015986j
Date:
22-Feb-01     Release date:   22-Oct-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P06239  (LCK_HUMAN) -  Tyrosine-protein kinase Lck
Seq:
Struc:
509 a.a.
63 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.7.10.2  - Non-specific protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP
+ [protein]-L-tyrosine
= ADP
+ [protein]-L-tyrosine phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1021/bi015986j Biochemistry 41:5120-5130 (2002)
PubMed id: 11955060  
 
 
Structural investigation of the binding of a herpesviral protein to the SH3 domain of tyrosine kinase Lck.
K.Schweimer, S.Hoffmann, F.Bauer, U.Friedrich, C.Kardinal, S.M.Feller, B.Biesinger, H.Sticht.
 
  ABSTRACT  
 
Herpesvirus saimiri codes for a tyrosine kinase interacting protein (Tip) that interacts with both the SH3 domain and the kinase domain of the T-cell-specific tyrosine kinase Lck via two separate motifs. The activation of Lck by Tip is considered as a key event in the transformation of human T-lymphocytes during herpesviral infection. We investigated the interaction of proline-rich Tip peptides with the LckSH3 domain starting with the structural characterization of the unbound interaction partners. The solution structure of the LckSH3 was determined by heteronuclear multidimensional nuclear magnetic resonance (NMR) spectroscopy using 44 residual dipolar couplings in addition to the conventional experimental restraints. Circular dichroism spectroscopy proved that the polyproline helix of Tip is already formed prior to SH3 binding and is conformationally stable. NMR titration experiments point out three major regions of the Tip-Lck interaction comprising the RT loop, the n-src loop, and a helical turn preceding the last strand of the beta-sheet. Further changes of the chemical shifts were observed for the N- and C-terminal beta-strands of the SH3 domain, indicating additional contacts outside the proline-rich segment or subtle structural rearrangements transmitted from the binding site of the proline helix. Fluorescence spectroscopy shows that Tip binds to the SH3 domains of several Src kinases (Lck, Hck, Lyn, Src, Fyn, Yes), exhibiting the highest affinities for Lyn, Hck, and Lck.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21345171 B.M.Burmann, U.Scheckenhofer, K.Schweimer, and P.Rösch (2011).
Domain interactions of the transcription-translation coupling factor Escherichia coli NusG are intermolecular and transient.
  Biochem J, 435, 783-789.  
20024074 S.Hoffmann, S.A.Funke, K.Wiesehan, S.Moedder, J.M.Glück, S.Feuerstein, M.Gerdts, J.Mötter, and D.Willbold (2010).
Competitively selected protein ligands pay their increase in specificity by a decrease in affinity.
  Mol Biosyst, 6, 116-123.  
19290556 A.Leal, K.Huehne, F.Bauer, H.Sticht, P.Berger, U.Suter, B.Morera, G.Del Valle, J.R.Lupski, A.Ekici, F.Pasutto, S.Endele, R.Barrantes, C.Berghoff, M.Berghoff, B.Neundörfer, D.Heuss, T.Dorn, P.Young, L.Santolin, T.Uhlmann, M.Meisterernst, M.Sereda, G.M.Zu Horste, K.A.Nave, A.Reis, and B.Rautenstrauss (2009).
Identification of the variant Ala335Val of MED25 as responsible for CMT2B2: molecular data, functional studies of the SH3 recognition motif and correlation between wild-type MED25 and PMP22 RNA levels in CMT1A animal models.
  Neurogenetics, 10, 275-287.  
19150358 R.D.Shereda, N.J.Reiter, S.E.Butcher, and J.L.Keck (2009).
Identification of the SSB binding site on E. coli RecQ reveals a conserved surface for binding SSB's C terminus.
  J Mol Biol, 386, 612-625.  
18186541 M.Wittlich, B.W.Koenig, and D.Willbold (2008).
Structural consequences of phosphorylation of two serine residues in the cytoplasmic domain of HIV-1 VpU.
  J Pept Sci, 14, 804-810.  
17207813 J.L.Mitchell, R.P.Trible, L.A.Emert-Sedlak, D.D.Weis, E.C.Lerner, J.J.Applen, B.M.Sefton, T.E.Smithgall, and J.R.Engen (2007).
Functional characterization and conformational analysis of the Herpesvirus saimiri Tip-C484 protein.
  J Mol Biol, 366, 1282-1293.  
17008721 D.D.Weis, P.Kjellen, B.M.Sefton, and J.R.Engen (2006).
Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip.
  Protein Sci, 15, 2402-2410.  
16891373 H.X.Zhou (2006).
Quantitative relation between intermolecular and intramolecular binding of pro-rich peptides to SH3 domains.
  Biophys J, 91, 3170-3181.  
16956971 M.Zeeb, K.E.Max, U.Weininger, C.Löw, H.Sticht, and J.Balbach (2006).
Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution.
  Nucleic Acids Res, 34, 4561-4571.
PDB code: 2f52
16600966 V.Musi, B.Birdsall, G.Fernandez-Ballester, R.Guerrini, S.Salvatori, L.Serrano, and A.Pastore (2006).
New approaches to high-throughput structure characterization of SH3 complexes: the example of Myosin-3 and Myosin-5 SH3 domains from S. cerevisiae.
  Protein Sci, 15, 795-807.
PDB code: 2btt
15987884 A.Eisenmann, S.Schwarz, S.Prasch, K.Schweimer, and P.Rösch (2005).
The E. coli NusA carboxy-terminal domains are structurally similar and show specific RNAP- and lambdaN interaction.
  Protein Sci, 14, 2018-2029.
PDB codes: 1wcl 1wcn
15389624 A.Y.Tsygankov (2005).
Cell transformation by Herpesvirus saimiri.
  J Cell Physiol, 203, 305-318.  
16155203 F.Bauer, K.Schweimer, H.Meiselbach, S.Hoffmann, P.Rösch, and H.Sticht (2005).
Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity.
  Protein Sci, 14, 2487-2498.
PDB code: 1w1f
15976924 L.Briese, A.Preusser, and D.Willbold (2005).
Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.
  J Biomed Sci, 12, 451-456.  
14593111 U.Breitinger, H.G.Breitinger, F.Bauer, K.Fahmy, D.Glockenhammer, and C.M.Becker (2004).
Conserved high affinity ligand binding and membrane association in the native and refolded extracellular domain of the human glycine receptor alpha1-subunit.
  J Biol Chem, 279, 1627-1636.  
12734017 L.Briese, and D.Willbold (2003).
Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy.
  BMC Struct Biol, 3, 3.
PDB code: 1kik
12707255 T.Lauber, P.Neudecker, P.Rösch, and U.C.Marx (2003).
Solution structure of human proguanylin: the role of a hormone prosequence.
  J Biol Chem, 278, 24118-24124.
PDB code: 1o8r
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.