1svy

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{{STRUCTURE_1svy| PDB=1svy | SCENE= }}
{{STRUCTURE_1svy| PDB=1svy | SCENE= }}
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'''SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE'''
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===SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE===
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==Overview==
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The crystal structure of the F-actin binding domain 2 of severin, the gelsolin homologue from Dictyostelium discoideum, has been determined by multiple isomorphous replacement and refined to 1.75 A resolution. The structure reveals an alpha-helix-beta-sheet sandwich similar to the domains of gelsolin and villin, and contains two cation-binding sites, as observed in other domain 1 and domain 2 homologues. Comparison of the structures of several gelsolin family domains has identified residues that may mediate F-actin binding in gelsolin domain 2 homologues. To assess the involvement of these residues in F-actin binding, three mutants of human gelsolin domain 2 were assayed for F-actin binding activity and thermodynamic stability. Two of the mutants, RRV168AAA and RLK210AAA, demonstrated a lowered affinity for F-actin, indicating a role for those residues in filament binding. Using both structural and biochemical data, we have constructed a model of the gelsolin domain 1-domain 2-F-actin complex. This model highlights a number of interactions that may serve as positive and negative determinants of filament end- and side-binding.
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{{ABSTRACT_PUBMED_10820002}}
==About this Structure==
==About this Structure==
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[[Category: Severin]]
[[Category: Severin]]
[[Category: Villin]]
[[Category: Villin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:24:54 2008''

Revision as of 21:24, 27 July 2008

Template:STRUCTURE 1svy

SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE

Template:ABSTRACT PUBMED 10820002

About this Structure

1SVY is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.

Reference

Mapping the functional surface of domain 2 in the gelsolin superfamily., Puius YA, Fedorov EV, Eichinger L, Schleicher M, Almo SC, Biochemistry. 2000 May 9;39(18):5322-31. PMID:10820002

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