2eyn: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= ACTN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ACTN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2eyi|2EYI]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2eyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eyn OCA], [http://www.ebi.ac.uk/pdbsum/2eyn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2eyn RCSB]</span> | |||
}} | }} | ||
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[[Category: structural protein]] | [[Category: structural protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:55:29 2008'' | ||
Revision as of 02:55, 31 March 2008
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| , resolution 1.800Å | |||||||
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| Gene: | ACTN1 (Homo sapiens) | ||||||
| Related: | 2EYI
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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