2a41: Difference between revisions
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'''Ternary complex of the WH2 Domain of WIP with Actin-DNAse I''' | '''Ternary complex of the WH2 Domain of WIP with Actin-DNAse I''' | ||
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[[Category: Dominguez, R.]] | [[Category: Dominguez, R.]] | ||
[[Category: Kerff, F.]] | [[Category: Kerff, F.]] | ||
[[Category: | [[Category: Actin]] | ||
[[Category: | [[Category: Arp2/3]] | ||
[[Category: | [[Category: Dnase i]] | ||
[[Category: | [[Category: Wasp]] | ||
[[Category: | [[Category: Wh2]] | ||
[[Category: | [[Category: Wip]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:34:35 2008'' | |||
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Revision as of 18:34, 3 May 2008
Ternary complex of the WH2 Domain of WIP with Actin-DNAse I
OverviewOverview
Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) is a small and widespread actin-binding motif. In the WASP family, WH2 plays a role in filament nucleation by Arp2/3 complex. Here we describe the crystal structures of complexes of actin with the WH2 domains of WASP, WASP-family verprolin homologous protein, and WASP-interacting protein. Despite low sequence identity, WH2 shares structural similarity with the N-terminal portion of the actin monomer-sequestering thymosin beta domain (Tbeta). We show that both domains inhibit nucleotide exchange by targeting the cleft between actin subdomains 1 and 3, a common binding site for many unrelated actin-binding proteins. Importantly, WH2 is significantly shorter than Tbeta but binds actin with approximately 10-fold higher affinity. WH2 lacks a C-terminal extension that in Tbeta4 becomes involved in monomer sequestration by interfering with intersubunit contacts in F-actin. Owing to their shorter length, WH2 domains connected in tandem by short linkers can coexist with intersubunit contacts in F-actin and are proposed to function in filament nucleation by lining up actin subunits along a filament strand. The WH2-central region of WASP-family proteins is proposed to function in an analogous way by forming a special class of tandem repeats whose function is to line up actin and Arp2 during Arp2/3 nucleation. The structures also suggest a mechanism for how profilin-binding Pro-rich sequences positioned N-terminal to WH2 could feed actin monomers directly to WH2, thereby playing a role in filament elongation.
About this StructureAbout this Structure
2A41 is a Protein complex structure of sequences from Bos taurus and Oryctolagus cuniculus. Full crystallographic information is available from OCA.
ReferenceReference
Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly., Chereau D, Kerff F, Graceffa P, Grabarek Z, Langsetmo K, Dominguez R, Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16644-9. Epub 2005 Nov 7. PMID:16275905 Page seeded by OCA on Sat May 3 18:34:35 2008