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1qc6

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(New page: 200px<br /><applet load="1qc6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qc6, resolution 2.6&Aring;" /> '''EVH1 domain from ENA/...)
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[[Image:1qc6.gif|left|200px]]<br /><applet load="1qc6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qc6.gif|left|200px]]<br /><applet load="1qc6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qc6, resolution 2.6&Aring;" />
caption="1qc6, resolution 2.6&Aring;" />
'''EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide'''<br />
'''EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide'''<br />
==Overview==
==Overview==
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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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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.
==About this Structure==
==About this Structure==
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1QC6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QC6 OCA].
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1QC6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QC6 OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Almo, S.C.]]
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[[Category: Almo, S C.]]
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[[Category: Fedorov, A.A.]]
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[[Category: Fedorov, A A.]]
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[[Category: Fedorov, E.V.]]
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[[Category: Fedorov, E V.]]
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[[Category: Gertler, F.B.]]
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[[Category: Gertler, F B.]]
[[Category: actin-based cell motility]]
[[Category: actin-based cell motility]]
[[Category: an incomplete seven stranded anti-parallel beta barrel closed by an alpha helix]]
[[Category: an incomplete seven stranded anti-parallel beta barrel closed by an alpha helix]]
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[[Category: interaction module]]
[[Category: interaction module]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:33:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:08 2008''

Revision as of 12:38, 21 February 2008

Image:1qc6.gif

1qc6, resolution 2.6Å

Drag the structure with the mouse to rotate

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

Overview

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.

About this Structure

1QC6 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

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

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