1p8z
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(New page: 200px<br /> <applet load="1p8z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p8z, resolution 2.60Å" /> '''Complex Between Rab...)
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Revision as of 16:34, 12 November 2007
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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 CD, CA and ATP 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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