2eyn: Difference between revisions
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'''Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution''' | '''Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution''' | ||
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[[Category: Lee, S H.]] | [[Category: Lee, S H.]] | ||
[[Category: Li, Y.]] | [[Category: Li, Y.]] | ||
[[Category: | [[Category: Actin-binding]] | ||
[[Category: | [[Category: Actin-bundling]] | ||
[[Category: | [[Category: Actin-crosslinking]] | ||
[[Category: | [[Category: Calponin homology domain]] | ||
[[Category: | [[Category: Ch domain]] | ||
[[Category: | [[Category: Structural protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:15:29 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 03:15, 4 May 2008
Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution
OverviewOverview
Alpha-actinin belongs to the spectrin family of actin crosslinking and bundling proteins that function as key regulators of cell motility, morphology and adhesion. The actin-binding domain (ABD) of these proteins consists of two consecutive calponin homology (CH) domains. Electron microscopy studies on ABDs appear to support two competing actin-binding models, extended and compact, whereas the crystal structures typically display a compact conformation. We have determined the 1.7A resolution structure of the ABD of alpha-actinin 1, a ubiquitously expressed isoform. The structure displays the classical compact conformation. We evaluated the two binding models by surface conservation analysis. The results show a conserved surface that spans both domains and corresponds to two previously identified actin-binding sites (ABS2 and ABS3). A third, and probably less important site, ABS1, is mostly buried in the compact conformation. However, a thorough examination of existing structures suggests a weak and semi-polar binding interface between the two CHs, leaving open the possibility of domain reorientation or opening. Our results are consistent with a two-step binding mechanism in which the ABD interacts first in the compact form observed in the structures, and then transitions toward a higher affinity state, possibly through minor rearrangement of the domains.
About this StructureAbout this Structure
2EYN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the actin-binding domain of alpha-actinin 1: evaluating two competing actin-binding models., Borrego-Diaz E, Kerff F, Lee SH, Ferron F, Li Y, Dominguez R, J Struct Biol. 2006 Aug;155(2):230-8. Epub 2006 Apr 25. PMID:16698282 Page seeded by OCA on Sun May 4 03:15:29 2008