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PDBsum entry 1evh
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Contractile protein PDB id
1evh

 

 

 

 

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Contents
Protein chain
111 a.a. *
Ligands
ACE-PHE-PRO-PRO-
PRO-PRO
Waters ×27
* Residue conservation analysis
PDB id:
1evh
Name: Contractile protein
Title: Evh1 domain from murine enabled in complex with acta peptide
Structure: Protein (mena evh1 domain). Chain: a. Fragment: mena 1-112. Synonym: wh1 domain. Engineered: yes. Peptide acta. Chain: b. Fragment: proline rich repeat. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Organ: brain. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: sequence from listeria monocytogenes
Biol. unit: Tetramer (from PQS)
Resolution:
1.80Å     R-factor:   0.230     R-free:   0.268
Authors: K.E.Prehoda,D.J.Lee,W.A.Lim
Key ref:
K.E.Prehoda et al. (1999). Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly. Cell, 97, 471-480. PubMed id: 10338211 DOI: 10.1016/S0092-8674(00)80757-6
Date:
21-Apr-99     Release date:   21-May-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q03173  (ENAH_MOUSE) -  Protein enabled homolog from Mus musculus
Seq:
Struc: 		 
Seq:
Struc: 		802 a.a.
111 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1016/S0092-8674(00)80757-6 Cell 97:471-480 (1999)
PubMed id: 10338211  
 
 
Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly.
K.E.Prehoda, D.J.Lee, W.A.Lim.
 
  ABSTRACT  
 
The Enabled/VASP homology 1 (EVH1; also called WH1) domain is an interaction module found in several proteins implicated in actin-based cell motility. EVH1 domains bind the consensus proline-rich motif FPPPP and are required for targeting the actin assembly machinery to sites of cytoskeletal remodeling. The crystal structure of the mammalian Enabled (Mena) EVH1 domain complexed with a peptide ligand reveals a mechanism of recognition distinct from that used by other proline-binding modules. The EVH1 domain fold is unexpectedly similar to that of the pleckstrin homology domain, a membrane localization module. This finding demonstrates the functional plasticity of the pleckstrin homology fold as a binding scaffold and suggests that membrane association may play an auxiliary role in EVH1 targeting.
 
  Selected figure(s)  
 
Figure 4.
Figure 4. Mechanism of Proline-Rich Peptide Recognition by EVH1 Domains(A) The peptide ligand (magenta) adopts a PPII-helical conformation and docks into a V-shaped groove on the domain surface (green). The orientation shown is approximately the same as that shown in Figure 3A.(B) Close-up bird’s-eye view of peptide ligand docked against the conserved EVH1 domain aromatic triad (green side chains). PPII-helical axis of the ligand is oriented vertically.(C) Schematic comparison of EVH1 complex (same orientation as in [A]) and SH3 complex. Both domains use a series of aromatic side chains (planar protrusions) for recognition, but their different arrangement caused the PPII-helical ligand (triangular prism) to dock in different orientations. SH3 recognition focuses on one surface of the PPII helix and therefore absolutely requires prolines at sites labeled 2 and 5. EVH1 recognition focuses more on the overall shape of the helix and therefore shows only an overall preference for proline residues at all positions. Recognition interfaces of WW domains and profilin resemble the SH3 surface.(D) Region of the Mena EVH1 domain that may interact with C-terminal acidic residues from ActA-derived ligands. A highly electropositive region (blue) is found immediately adjacent to the C terminus of the bound core peptide. Potential path of the continuing peptide chain is indicated by magenta spheres. Figure was generated using GRASP, Molscript, and RASTER3D.
Figure 6.
Figure 6. Possible Mechanism for EVH1 Domain Targeting of Actin Assembly(A) EVH1 proteins may recognize proline-rich peptides (solid rectangle) in an acidic phospholipid context to selectively localize to leading edge membrane sites.(B) Pathogens such as Listeria monocytogenes may use peptide ligand sequences that emulate the combination of interactions described in (A). The ActA sequences have a high density of negatively charged residues immediately C-terminal to the peptide’s proline-rich core peptide sequence. Such ligands have higher affinity than host-derived ligands and may constitutively recruit EVH1 domain proteins in a nonmembrane context (e.g., outside of the cell wall of the gram-positive bacteria).
 
  The above figures are reprinted by permission from Cell Press: Cell (1999, 97, 471-480) copyright 1999.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
23142987 J.E.Braun, V.Truffault, A.Boland, E.Huntzinger, C.T.Chang, G.Haas, O.Weichenrieder, M.Coles, and E.Izaurralde (2012).
A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5' exonucleolytic degradation.
  Nat Struct Mol Biol, 19, 1324-1331.
PDB code: 2lyd
21041447 S.D.Hansen, and R.D.Mullins (2010).
VASP is a processive actin polymerase that requires monomeric actin for barbed end association.
  J Cell Biol, 191, 571-584.  
19893486 S.Terawaki, K.Kitano, T.Mori, Y.Zhai, Y.Higuchi, N.Itoh, T.Watanabe, K.Kaibuchi, and T.Hakoshima (2010).
The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding module.
  EMBO J, 29, 236-250.
PDB codes: 3a8n 3a8p 3a8q
19666464 F.Campa, H.Y.Yoon, V.L.Ha, Z.Szentpetery, T.Balla, and P.A.Randazzo (2009).
A PH domain in the Arf GTPase-activating protein (GAP) ARAP1 binds phosphatidylinositol 3,4,5-trisphosphate and regulates Arf GAP activity independently of recruitment to the plasma membranes.
  J Biol Chem, 284, 28069-28083.  
19284291 N.M.Link, C.Hunke, J.W.Mueller, J.Eichler, and P.Bayer (2009).
The solution structure of pGolemi, a high affinity Mena EVH1 binding miniature protein, suggests explanations for paralog-specific binding to Ena/VASP homology (EVH) 1 domains.
  Biol Chem, 390, 417-426.
PDB code: 2k76
18985426 S.Goswami, U.Philippar, D.Sun, A.Patsialou, J.Avraham, W.Wang, F.Di Modugno, P.Nistico, F.B.Gertler, and J.S.Condeelis (2009).
Identification of invasion specific splice variants of the cytoskeletal protein Mena present in mammary tumor cells during invasion in vivo.
  Clin Exp Metastasis, 26, 153-159.  
18246036 J.V.Small (2008).
Facing up to Mena: Tes(ting) times for EVH1 domains.
  Nat Cell Biol, 10, 118-120.  
19112510 S.C.Graham, R.Assenberg, O.Delmas, A.Verma, A.Gholami, C.Talbi, R.J.Owens, D.I.Stuart, J.M.Grimes, and H.Bourhy (2008).
Rhabdovirus matrix protein structures reveal a novel mode of self-association.
  PLoS Pathog, 4, e1000251.
PDB codes: 2w2r 2w2s
18158903 B.Boëda, D.C.Briggs, T.Higgins, B.K.Garvalov, A.J.Fadden, N.Q.McDonald, and M.Way (2007).
Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding.
  Mol Cell, 28, 1071-1082.
PDB code: 2iyb
17229736 F.C.Peterson, Q.Deng, M.Zettl, K.E.Prehoda, W.A.Lim, M.Way, and B.F.Volkman (2007).
Multiple WASP-interacting protein recognition motifs are required for a functional interaction with N-WASP.
  J Biol Chem, 282, 8446-8453.
PDB code: 2ifs
17914456 F.Ferron, G.Rebowski, S.H.Lee, and R.Dominguez (2007).
Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP.
  EMBO J, 26, 4597-4606.
PDB codes: 2pav 2pbd
17973491 J.H.Holtzman, K.Woronowicz, D.Golemi-Kotra, and A.Schepartz (2007).
Miniature protein ligands for EVH1 domains: interplay between affinity, specificity, and cell motility.
  Biochemistry, 46, 13541-13553.  
17935994 M.Sheffield, T.Loveless, J.Hardin, and J.Pettitt (2007).
C. elegans Enabled exhibits novel interactions with N-WASP, Abl, and cell-cell junctions.
  Curr Biol, 17, 1791-1796.  
16810654 C.Hunke, T.Hirsch, and J.Eichler (2006).
Structure-based synthetic mimicry of discontinuous protein binding sites: inhibitors of the interaction of Mena EVH1 domain with proline-rich ligands.
  Chembiochem, 7, 1258-1264.  
16221668 D.F.Ceccarelli, H.K.Song, F.Poy, M.D.Schaller, and M.J.Eck (2006).
Crystal structure of the FERM domain of focal adhesion kinase.
  J Biol Chem, 281, 252-259.
PDB codes: 2aeh 2al6
16899512 S.A.Myers, L.R.Leeper, and C.Y.Chung (2006).
WASP-interacting protein is important for actin filament elongation and prompt pseudopod formation in response to a dynamic chemoattractant gradient.
  Mol Biol Cell, 17, 4564-4575.  
16652141 T.Yoshida, T.Hisamoto, J.Akiba, H.Koga, K.Nakamura, Y.Tokunaga, S.Hanada, H.Kumemura, M.Maeyama, M.Harada, H.Ogata, H.Yano, M.Kojiro, T.Ueno, A.Yoshimura, and M.Sata (2006).
Spreds, inhibitors of the Ras/ERK signal transduction, are dysregulated in human hepatocellular carcinoma and linked to the malignant phenotype of tumors.
  Oncogene, 25, 6056-6066.  
16049010 H.M.Patterson, J.A.Brannigan, S.M.Cutting, K.S.Wilson, A.J.Wilkinson, E.Ab, T.Diercks, R.N.de Jong, V.Truffault, G.E.Folkers, and R.Kaptein (2005).
The structure of bypass of forespore C, an intercompartmental signaling factor during sporulation in Bacillus.
  J Biol Chem, 280, 36214-36220.
PDB code: 2bw2
15778995 J.B.Xanthos, S.J.Wanner, and J.R.Miller (2005).
Cloning and developmental expression of Xenopus Enabled (Xena).
  Dev Dyn, 233, 631-637.  
15880548 L.J.Ball, R.Kühne, J.Schneider-Mergener, and H.Oschkinat (2005).
Recognition of Proline-Rich Motifs by Protein-Protein-Interaction Domains.
  Angew Chem Int Ed Engl, 44, 2852-2869.  
15869386 W.Cho, and R.V.Stahelin (2005).
Membrane-protein interactions in cell signaling and membrane trafficking.
  Annu Rev Biophys Biomol Struct, 34, 119-151.  
14757752 H.Akazawa, S.Kudoh, N.Mochizuki, N.Takekoshi, H.Takano, T.Nagai, and I.Komuro (2004).
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15477347 H.Wang, F.E.McCann, J.D.Gordan, X.Wu, M.Raab, T.H.Malik, D.M.Davis, and C.E.Rudd (2004).
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  J Exp Med, 200, 1063-1074.  
15280232 J.Withee, B.Galligan, N.Hawkins, and G.Garriga (2004).
Caenorhabditis elegans WASP and Ena/VASP proteins play compensatory roles in morphogenesis and neuronal cell migration.
  Genetics, 167, 1165-1176.  
15341735 K.Saito, T.Kigawa, S.Koshiba, K.Sato, Y.Matsuo, A.Sakamoto, T.Takagi, M.Shirouzu, T.Yabuki, E.Nunokawa, E.Seki, T.Matsuda, M.Aoki, Y.Miyata, N.Hirakawa, M.Inoue, T.Terada, T.Nagase, R.Kikuno, M.Nakayama, O.Ohara, A.Tanaka, and S.Yokoyama (2004).
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PDB code: 1ixd
15456751 M.Pekkala, R.Hieta, U.Bergmann, K.I.Kivirikko, R.K.Wierenga, and J.Myllyharju (2004).
The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues.
  J Biol Chem, 279, 52255-52261.
PDB code: 1tjc
14758354 M.She, C.J.Decker, K.Sundramurthy, Y.Liu, N.Chen, R.Parker, and H.Song (2004).
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  Nat Struct Mol Biol, 11, 249-256.
PDB code: 1q67
15332112 Y.Le Page, F.Demay, and G.Salbert (2004).
A neural-specific splicing event generates an active form of the Wiskott-Aldrich syndrome protein.
  EMBO Rep, 5, 895-900.  
12837609 A.V.Kwiatkowski, F.B.Gertler, and J.J.Loureiro (2003).
Function and regulation of Ena/VASP proteins.
  Trends Cell Biol, 13, 386-392.  
12857736 J.Zimmermann, R.Kühne, R.Volkmer-Engert, T.Jarchau, U.Walter, H.Oschkinat, and L.J.Ball (2003).
Design of N-substituted peptomer ligands for EVH1 domains.
  J Biol Chem, 278, 36810-36818.  
14690607 K.F.Ahmad, A.Melnick, S.Lax, D.Bouchard, J.Liu, C.L.Kiang, S.Mayer, S.Takahashi, J.D.Licht, and G.G.Privé (2003).
Mechanism of SMRT corepressor recruitment by the BCL6 BTB domain.
  Mol Cell, 12, 1551-1564.
PDB codes: 1r28 1r29 1r2b
14612666 K.Imai, S.Nonoyama, and H.D.Ochs (2003).
WASP (Wiskott-Aldrich syndrome protein) gene mutations and phenotype.
  Curr Opin Allergy Clin Immunol, 3, 427-436.  
12672821 K.Tani, S.Sato, T.Sukezane, H.Kojima, H.Hirose, H.Hanafusa, and T.Shishido (2003).
Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase.
  J Biol Chem, 278, 21685-21692.  
14570581 M.Krause, E.W.Dent, J.E.Bear, J.J.Loureiro, and F.B.Gertler (2003).
Ena/VASP proteins: regulators of the actin cytoskeleton and cell migration.
  Annu Rev Cell Dev Biol, 19, 541-564.  
12805219 R.Grosse, J.W.Copeland, T.P.Newsome, M.Way, and R.Treisman (2003).
A role for VASP in RhoA-Diaphanous signalling to actin dynamics and SRF activity.
  EMBO J, 22, 3050-3061.  
12824157 R.Hieta, L.Kukkola, P.Permi, P.Pirilä, K.I.Kivirikko, I.Kilpeläinen, and J.Myllyharju (2003).
The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides.
  J Biol Chem, 278, 34966-34974.  
12872157 S.C.Panchal, D.A.Kaiser, E.Torres, T.D.Pollard, and M.K.Rosen (2003).
A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex.
  Nat Struct Biol, 10, 591-598.  
12529859 S.I.Anderson, B.Behrendt, L.M.Machesky, R.H.Insall, and G.B.Nash (2003).
Linked regulation of motility and integrin function in activated migrating neutrophils revealed by interference in remodelling of the cytoskeleton.
  Cell Motil Cytoskeleton, 54, 135-146.  
12517699 S.J.Winder (2003).
Structural insights into actin-binding, branching and bundling proteins.
  Curr Opin Cell Biol, 15, 14-22.  
12940993 V.Auerbuch, J.J.Loureiro, F.B.Gertler, J.A.Theriot, and D.A.Portnoy (2003).
Ena/VASP proteins contribute to Listeria monocytogenes pathogenesis by controlling temporal and spatial persistence of bacterial actin-based motility.
  Mol Microbiol, 49, 1361-1375.  
12445268 A.S.Sechi, J.Buer, J.Wehland, and M.Probst-Kepper (2002).
Changes in actin dynamics at the T-cell/APC interface: implications for T-cell anergy?
  Immunol Rev, 189, 98.  
12437929 B.F.Volkman, K.E.Prehoda, J.A.Scott, F.C.Peterson, and W.A.Lim (2002).
Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome.
  Cell, 111, 565-576.
PDB code: 1mke
12163465 D.A.Portnoy, V.Auerbuch, and I.J.Glomski (2002).
The cell biology of Listeria monocytogenes infection: the intersection of bacterial pathogenesis and cell-mediated immunity.
  J Cell Biol, 158, 409-414.  
12134088 J.J.Loureiro, D.A.Rubinson, J.E.Bear, G.A.Baltus, A.V.Kwiatkowski, and F.B.Gertler (2002).
Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration.
  Mol Biol Cell, 13, 2533-2546.  
11994738 M.B.Yaffe (2002).
Phosphotyrosine-binding domains in signal transduction.
  Nat Rev Mol Cell Biol, 3, 177-186.  
12372256 M.Zettl, and M.Way (2002).
The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct sequence motifs.
  Curr Biol, 12, 1617-1622.  
11792550 P.J.Renfranz, and M.C.Beckerle (2002).
Doing (F/L)PPPPs: EVH1 domains and their proline-rich partners in cell polarity and migration.
  Curr Opin Cell Biol, 14, 88.  
11498782 B.L.Langille (2001).
Morphologic responses of endothelium to shear stress: reorganization of the adherens junction.
  Microcirculation, 8, 195-206.  
11316610 C.Krawczyk, and J.M.Penninger (2001).
Molecular controls of antigen receptor clustering and autoimmunity.
  Trends Cell Biol, 11, 212-220.  
11905825 G.A.Koretzky, and P.S.Myung (2001).
Positive and negative regulation of T-cell activation by adaptor proteins.
  Nat Rev Immunol, 1, 95.  
11395419 H.N.Higgs, and T.D.Pollard (2001).
Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins.
  Annu Rev Biochem, 70, 649-676.  
11581288 J.Skoble, V.Auerbuch, E.D.Goley, M.D.Welch, and D.A.Portnoy (2001).
Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility.
  J Cell Biol, 155, 89.  
11729265 M.B.Goldberg (2001).
Actin-based motility of intracellular microbial pathogens.
  Microbiol Mol Biol Rev, 65, 595.  
11489888 M.P.Machner, C.Urbanke, M.Barzik, S.Otten, A.S.Sechi, J.Wehland, and D.W.Heinz (2001).
ActA from Listeria monocytogenes can interact with up to four Ena/VASP homology 1 domains simultaneously.
  J Biol Chem, 276, 40096-40103.  
11295557 M.Reinhard, T.Jarchau, and U.Walter (2001).
Actin-based motility: stop and go with Ena/VASP proteins.
  Trends Biochem Sci, 26, 243-249.  
  11598191 O.M.Mykkänen, M.Grönholm, M.Rönty, M.Lalowski, P.Salmikangas, H.Suila, and O.Carpén (2001).
Characterization of human palladin, a microfilament-associated protein.
  Mol Biol Cell, 12, 3060-3073.  
11527980 U.Padmanabhan, S.Dasgupta, B.B.Biswas, and D.Dasgupta (2001).
High affinity association of myo-inositol trisphosphates with phytase and its effect upon the catalytic potential of the enzyme.
  J Biol Chem, 276, 43635-43644.  
10851193 A.D.Frankel (2000).
Fitting peptides into the RNA world.
  Curr Opin Struct Biol, 10, 332-340.  
10851183 B.Xiao, J.C.Tu, and P.F.Worley (2000).
Homer: a link between neural activity and glutamate receptor function.
  Curr Opin Neurobiol, 10, 370-374.  
10747019 C.Zwahlen, S.C.Li, L.E.Kay, T.Pawson, and J.D.Forman-Kay (2000).
Multiple modes of peptide recognition by the PTB domain of the cell fate determinant Numb.
  EMBO J, 19, 1505-1515.
PDB code: 1ddm
10995437 H.N.Higgs, and T.D.Pollard (2000).
Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex.
  J Cell Biol, 150, 1311-1320.  
10798399 J.Beneken, J.C.Tu, B.Xiao, M.Nuriya, J.P.Yuan, P.F.Worley, and D.J.Leahy (2000).
Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition.
  Neuron, 26, 143-154.
PDB codes: 1ddv 1ddw
10892743 J.E.Bear, J.J.Loureiro, I.Libova, R.Fässler, J.Wehland, and F.B.Gertler (2000).
Negative regulation of fibroblast motility by Ena/VASP proteins.
  Cell, 101, 717-728.  
10940243 J.H.Hurley, and S.Misra (2000).
Signaling and subcellular targeting by membrane-binding domains.
  Annu Rev Biophys Biomol Struct, 29, 49-79.  
11052943 K.E.Prehoda, J.A.Scott, R.D.Mullins, and W.A.Lim (2000).
Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex.
  Science, 290, 801-806.  
10990454 L.J.Ball, R.Kühne, B.Hoffmann, A.Häfner, P.Schmieder, R.Volkmer-Engert, M.Hof, M.Wahl, J.Schneider-Mergener, U.Walter, H.Oschkinat, and T.Jarchau (2000).
Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity.
  EMBO J, 19, 4903-4914.
PDB codes: 1egx 1jng
10679439 L.M.Lanier, and F.B.Gertler (2000).
From Abl to actin: Abl tyrosine kinase and associated proteins in growth cone motility.
  Curr Opin Neurobiol, 10, 80-87.  
10847681 M.A.Pearson, D.Reczek, A.Bretscher, and P.A.Karplus (2000).
Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.
  Cell, 101, 259-270.
PDB code: 1ef1
11137023 M.A.Wear, D.A.Schafer, and J.A.Cooper (2000).
Actin dynamics: assembly and disassembly of actin networks.
  Curr Biol, 10, R891-R895.  
10930849 M.Barzik, W.D.Schubert, U.Carl, J.Wehland, and D.W.Heinz (2000).
Crystallization and preliminary X-ray analysis of the EVH1 domain of Vesl-2b.
  Acta Crystallogr D Biol Crystallogr, 56, 930-932.  
10931874 M.M.Parast, and C.A.Otey (2000).
Characterization of palladin, a novel protein localized to stress fibers and cell adhesions.
  J Cell Biol, 150, 643-656.  
  10637295 M.M.Petit, J.Fradelizi, R.M.Golsteyn, T.A.Ayoubi, B.Menichi, D.Louvard, W.J.Van de Ven, and E.Friederich (2000).
LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity.
  Mol Biol Cell, 11, 117-129.  
11080629 N.Blomberg, E.Baraldi, M.Sattler, M.Saraste, and M.Nilges (2000).
Structure of a PH domain from the C. elegans muscle protein UNC-89 suggests a novel function.
  Structure, 8, 1079-1087.
PDB code: 1fho
10940259 T.D.Pollard, L.Blanchoin, and R.D.Mullins (2000).
Molecular mechanisms controlling actin filament dynamics in nonmuscle cells.
  Annu Rev Biophys Biomol Struct, 29, 545-576.  
10831611 T.Hirota, T.Morisaki, Y.Nishiyama, T.Marumoto, K.Tada, T.Hara, N.Masuko, M.Inagaki, K.Hatakeyama, and H.Saya (2000).
Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor.
  J Cell Biol, 149, 1073-1086.  
10375521 I.G.Macara (1999).
Nuclear transport: randy couples.
  Curr Biol, 9, R436-R439.  
10607674 J.D.Forman-Kay, and T.Pawson (1999).
Diversity in protein recognition by PTB domains.
  Curr Opin Struct Biol, 9, 690-695.  
10427083 L.M.Machesky, and R.H.Insall (1999).
Signaling to actin dynamics.
  J Cell Biol, 146, 267-272.  
10511705 M.D.Welch (1999).
The world according to Arp: regulation of actin nucleation by the Arp2/3 complex.
  Trends Cell Biol, 9, 423-427.  
10467124 M.F.Carlier, A.Ducruix, and D.Pantaloni (1999).
Signalling to actin: the Cdc42-N-WASP-Arp2/3 connection.
  Chem Biol, 6, R235-R240.  
10542412 N.Blomberg, E.Baraldi, M.Nilges, and M.Saraste (1999).
The PH superfold: a structural scaffold for multiple functions.
  Trends Biochem Sci, 24, 441-445.  
10570153 S.Tadokoro, T.Tachibana, T.Imanaka, W.Nishida, and K.Sobue (1999).
Involvement of unique leucine-zipper motif of PSD-Zip45 (Homer 1c/vesl-1L) in group 1 metabotropic glutamate receptor clustering.
  Proc Natl Acad Sci U S A, 96, 13801-13806.  
10542409 T.M.Svitkina, and G.G.Borisy (1999).
Progress in protrusion: the tell-tale scar.
  Trends Biochem Sci, 24, 432-436.  
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.

 

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