2eyi
From Proteopedia
(New page: 200px<br /> <applet load="2eyi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2eyi, resolution 1.700Å" /> '''Crystal structure ...) |
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| - | [[Image:2eyi.gif|left|200px]]<br /> | + | [[Image:2eyi.gif|left|200px]]<br /><applet load="2eyi" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="2eyi, resolution 1.700Å" /> | caption="2eyi, resolution 1.700Å" /> | ||
'''Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.7 Angstrom resolution'''<br /> | '''Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.7 Angstrom resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Alpha-actinin belongs to the spectrin family of actin crosslinking and | + | 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 Structure== | ==About this Structure== | ||
| - | 2EYI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2EYI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EYI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ferron, F.]] | [[Category: Ferron, F.]] | ||
[[Category: Kerff, F.]] | [[Category: Kerff, F.]] | ||
| - | [[Category: Lee, S | + | [[Category: Lee, S H.]] |
[[Category: Li, Y.]] | [[Category: Li, Y.]] | ||
[[Category: actin-binding]] | [[Category: actin-binding]] | ||
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[[Category: structural protein]] | [[Category: structural protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:53 2008'' |
Revision as of 15:15, 21 February 2008
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Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.7 Angstrom resolution
Overview
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 Structure
2EYI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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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