1mb8
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(New page: 200px<br /> <applet load="1mb8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mb8, resolution 2.15Å" /> '''Crystal Structure o...)
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Revision as of 16:03, 12 November 2007
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Crystal Structure of the actin binding domain of plectin
Contents |
Overview
Plectin is a widely expressed cytoskeletal linker. Here we report the, crystal structure of the actin binding domain of plectin and show that, this region is sufficient for interaction with F-actin or the cytoplasmic, region of integrin alpha6beta4. The structure is formed by two calponin, homology domains arranged in a closed conformation. We show that binding, to F-actin induces a conformational change in plectin that is inhibited by, an engineered interdomain disulfide bridge. A two-step induced fit, mechanism involving binding and subsequent domain rearrangement is, proposed. In contrast, interaction with integrin alpha6beta4 occurs in a, closed conformation. Competitive binding of plectin to F-actin and, integrin alpha6beta4 may rely on the observed alternative binding, mechanisms and involve both allosteric and steric factors.
Disease
Known diseases associated with this structure: Epidermolysis bullosa simplex, Ogna type OMIM:[601282], Muscular dystrophy with epidermolysis bullosa simplex OMIM:[601282]
About this Structure
1MB8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4., Garcia-Alvarez B, Bobkov A, Sonnenberg A, de Pereda JM, Structure. 2003 Jun;11(6):615-25. PMID:12791251
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