1svy: Difference between revisions

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[[Image:1svy.gif|left|200px]]
[[Image:1svy.gif|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1svy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svy OCA], [http://www.ebi.ac.uk/pdbsum/1svy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1svy RCSB]</span>
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'''SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE'''
'''SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE'''
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[[Category: Schleicher, M.]]
[[Category: Schleicher, M.]]
[[Category: Sullivan, M.]]
[[Category: Sullivan, M.]]
[[Category: actin-binding protein]]
[[Category: Actin-binding protein]]
[[Category: calcium]]
[[Category: Calcium]]
[[Category: calcium-binding]]
[[Category: Calcium-binding]]
[[Category: cytoskeleton]]
[[Category: Cytoskeleton]]
[[Category: gelsolin]]
[[Category: Gelsolin]]
[[Category: pip2]]
[[Category: Pip2]]
[[Category: severin]]
[[Category: Severin]]
[[Category: villin]]
[[Category: Villin]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:40 2008''

Revision as of 09:12, 3 May 2008

File:1svy.gif

Template:STRUCTURE 1svy

SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE


OverviewOverview

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.

About this StructureAbout this Structure

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

ReferenceReference

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 Page seeded by OCA on Sat May 3 09:12:01 2008

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