2eyn: Difference between revisions

Revision as of 16:38, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2eyn.png

Template:STRUCTURE 2eyn

Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolutionCrystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution

Template:ABSTRACT PUBMED 16698282

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 Tue Jul 29 16:38:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2eyn.gif|left|200px]]
+{{Seed}}
+[[Image:2eyn.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2eyn|  PDB=2eyn  |  SCENE=  }}
-'''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===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16698282}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16698282 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16698282}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Ch domain]]
 [[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 Tue Jul 29 16:38:00 2008''