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Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function

Nature Structural Biology volume 6, pages 661–665 (1999)Cite this article

Abstract

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.

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Figure 1: Structure of the EVL EVH1–peptide complex.
Figure 2: Alignment of EVH1, PH and PTB domains.
Figure 3: Comparison of proteins that display the EVH1/PH/PTB fold.

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Acknowledgements

We acknowledge the support of the National Institutes of Health (S.C.A. and F.B.G.).

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Authors and Affiliations

  1. Department of Biochemistry, Albert Einstein College of Medicine, Bronx, 10461, New York

    Alexander A. Fedorov, Elena Fedorov & Steven C. Almo

  2. Department of Biology and Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, 02142, Massachusetts

    Frank Gertler

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  1. Alexander A. Fedorov
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  2. Elena Fedorov
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  3. Frank Gertler
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  4. Steven C. Almo
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Fedorov, A., Fedorov, E., Gertler, F. et al. Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function. Nat Struct Mol Biol 6, 661–665 (1999). https://doi.org/10.1038/10717

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