1p8z
From Proteopedia
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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
Page seeded by OCA on Fri Feb 15 16:39:17 2008
