1p8z

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==Overview==
==Overview==
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We present the 2.6 A resolution crystal structure of a complex formed, between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure, differs from those of other gelsolin domain 1 (G1) complexes in that an, additional six amino acid residues from the crucial linker region into, gelsolin domain 2 (G2) are visible and are attached securely to the, surface of actin. The linker segment extends away from G1 up the face of, actin in a direction that infers G2 will bind along the same long-pitch, helical strand as the actin bound to G1. This is consistent with a, mechanism whereby G2 attaches gelsolin to the side of a filament and then, directs G1 toward a position where it would disrupt actin-actin contacts., Alignment of the sequence of the structurally important residues within, the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein, family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin, beta4) suggests that the opposing activities of filament assembly and, disassembly may exploit a common patch on the surface of actin.
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We present the 2.6 A resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin.
==Disease==
==Disease==
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[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Burtnick, L.D.]]
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[[Category: Burtnick, L D.]]
[[Category: Irobi, E.]]
[[Category: Irobi, E.]]
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[[Category: Robinson, R.C.]]
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[[Category: Robinson, R C.]]
[[Category: ATP]]
[[Category: ATP]]
[[Category: CA]]
[[Category: CA]]
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[[Category: linker between gelsolin domain 1 and domain 2]]
[[Category: linker between gelsolin domain 1 and domain 2]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:39:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:29 2008''

Revision as of 12:26, 21 February 2008


1p8z, resolution 2.60Å

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Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu156

Contents

Overview

We present the 2.6 A resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin.

Disease

Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[137350]

About this Structure

1P8Z is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus with , and as ligands. Full crystallographic information is available from OCA.

Reference

From the first to the second domain of gelsolin: a common path on the surface of actin?, Irobi E, Burtnick LD, Urosev D, Narayan K, Robinson RC, FEBS Lett. 2003 Sep 25;552(2-3):86-90. PMID:14527665

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