1qc6

EVH1 domain from ENA/VASP-like protein in complex with ACTA peptideEVH1 domain from ENA/VASP-like protein in complex with ACTA peptide

Structural highlights

1qc6 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EVL_MOUSE Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The Ena-VASP homology (EVH1) domain is a protein interaction module found in several proteins that are involved in transducing migratory and morphological signals into cytoskeletal reorganization. EVH1 specifically recognizes proline-rich sequences in its binding partners and directs the localization and formation of multicomponent assemblies involved in actin-based motile processes and neural development. The structure of the complex between an EVH1 domain and the target peptide sequence EFPPPPT identifies the interactions responsible for recognition and distinguishes it from other proline-rich binding modules, including SH3 and WW domains. Surprisingly, the EVH1 domain has structural similarity to pleckstrin homology (PH), phosphotyrosine-binding (PTB) and ran-binding (RanBD) domains.

Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function.,Fedorov AA, Fedorov E, Gertler F, Almo SC Nat Struct Biol. 1999 Jul;6(7):661-5. PMID:10404224^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lambrechts A, Kwiatkowski AV, Lanier LM, Bear JE, Vandekerckhove J, Ampe C, Gertler FB. cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains. J Biol Chem. 2000 Nov 17;275(46):36143-51. PMID:10945997 doi:http://dx.doi.org/10.1074/jbc.M006274200
↑ Laurent V, Loisel TP, Harbeck B, Wehman A, Grobe L, Jockusch BM, Wehland J, Gertler FB, Carlier MF. Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. J Cell Biol. 1999 Mar 22;144(6):1245-58. PMID:10087267
↑ Fedorov AA, Fedorov E, Gertler F, Almo SC. Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function. Nat Struct Biol. 1999 Jul;6(7):661-5. PMID:10404224 doi:10.1038/10717

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OCA

[1] Lambrechts A, Kwiatkowski AV, Lanier LM, Bear JE, Vandekerckhove J, Ampe C, Gertler FB. cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains. J Biol Chem. 2000 Nov 17;275(46):36143-51. PMID:10945997 doi:http://dx.doi.org/10.1074/jbc.M006274200

[2] Laurent V, Loisel TP, Harbeck B, Wehman A, Grobe L, Jockusch BM, Wehland J, Gertler FB, Carlier MF. Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. J Cell Biol. 1999 Mar 22;144(6):1245-58. PMID:10087267

[3] Fedorov AA, Fedorov E, Gertler F, Almo SC. Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function. Nat Struct Biol. 1999 Jul;6(7):661-5. PMID:10404224 doi:10.1038/10717

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