1p8x

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[[Image:1p8x.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1p8x", creates the "Structure Box" on the page.
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{{STRUCTURE_1p8x| PDB=1p8x | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p8x OCA], [http://www.ebi.ac.uk/pdbsum/1p8x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p8x RCSB]</span>
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'''The Calcium-Activated C-terminal half of gelsolin'''
'''The Calcium-Activated C-terminal half of gelsolin'''
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[[Category: Narayan, K.]]
[[Category: Narayan, K.]]
[[Category: Robinson, R C.]]
[[Category: Robinson, R C.]]
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[[Category: calcium-binding]]
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[[Category: Calcium-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:49:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:56:33 2008''
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Revision as of 01:49, 3 May 2008

Image:1p8x.gif

Template:STRUCTURE 1p8x

The Calcium-Activated C-terminal half of gelsolin


Overview

Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 A resolution in the presence of Ca(2+) ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca(2+) sites occupied. Neither actin nor the type-l Ca(2+), which normally is sandwiched between actin and G4, is required to achieve this conformation.

About this Structure

1P8X is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin., Narayan K, Chumnarnsilpa S, Choe H, Irobi E, Urosev D, Lindberg U, Schutt CE, Burtnick LD, Robinson RC, FEBS Lett. 2003 Sep 25;552(2-3):82-5. PMID:14527664 Page seeded by OCA on Sat May 3 04:49:55 2008

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