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1y2o

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[[Image:1y2o.gif|left|200px]]
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{{STRUCTURE_1y2o| PDB=1y2o | SCENE= }}
{{STRUCTURE_1y2o| PDB=1y2o | SCENE= }}
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'''Structure of N-terminal domain IRSp53/BAIAP2'''
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===Structure of N-terminal domain IRSp53/BAIAP2===
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==Overview==
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The scaffolding protein insulin receptor tyrosine kinase substrate p53 (IRSp53), a ubiquitous regulator of the actin cytoskeleton, mediates filopodia formation under the control of Rho-family GTPases. IRSp53 comprises a central SH3 domain, which binds to proline-rich regions of a wide range of actin regulators, and a conserved N-terminal IRSp53/MIM homology domain (IMD) that harbours F-actin-bundling activity. Here, we present the crystal structure of this novel actin-bundling domain revealing a coiled-coil domain that self-associates into a 180 A-long zeppelin-shaped dimer. Sedimentation velocity experiments confirm the presence of a single molecular species of twice the molecular weight of the monomer in solution. Mutagenesis of conserved basic residues at the extreme ends of the dimer abrogated actin bundling in vitro and filopodia formation in vivo, demonstrating that IMD-mediated actin bundling is required for IRSp53-induced filopodia formation. This study promotes an expanded view of IRSp53 as an actin regulator that integrates scaffolding and effector functions.
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The line below this paragraph, {{ABSTRACT_PUBMED_15635447}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15635447 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15635447}}
==About this Structure==
==About this Structure==
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[[Category: Cell motility]]
[[Category: Cell motility]]
[[Category: Filopodia]]
[[Category: Filopodia]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:48:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:33:03 2008''

Revision as of 19:33, 27 July 2008

Image:1y2o.png

Template:STRUCTURE 1y2o

Structure of N-terminal domain IRSp53/BAIAP2

Template:ABSTRACT PUBMED 15635447

About this Structure

1Y2O is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53., Millard TH, Bompard G, Heung MY, Dafforn TR, Scott DJ, Machesky LM, Futterer K, EMBO J. 2005 Jan 26;24(2):240-50. Epub 2005 Jan 6. PMID:15635447

Page seeded by OCA on Sun Jul 27 22:33:03 2008

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