This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2eyn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2eyn.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2eyn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2eyn| PDB=2eyn | SCENE= }}
{{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==
==About this Structure==
Line 34: Line 38:
[[Category: Ch domain]]
[[Category: Ch domain]]
[[Category: Structural protein]]
[[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''

Revision as of 13:38, 29 July 2008

Image:2eyn.png

Template:STRUCTURE 2eyn

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

Template:ABSTRACT PUBMED 16698282

About this Structure

2EYN 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

Page seeded by OCA on Tue Jul 29 16:38:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2eyn"
Personal tools