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.


1h6g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1h6g.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1h6g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1h6g| PDB=1h6g | SCENE= }}
{{STRUCTURE_1h6g| PDB=1h6g | SCENE= }}
-
'''ALPHA-CATENIN M-DOMAIN'''
+
===ALPHA-CATENIN M-DOMAIN===
-
==Overview==
+
<!--
-
The cytoskeletal protein alpha-catenin, which shares structural similarity with vinculin, is required for cadherin-mediated cell adhesion, and functions to modulate cell adhesive strength and to link the cadherins to the actin-based cytoskeleton. Here we describe the crystal structure of a region of alpha-catenin (residues 377-633) termed the M-fragment. The M-fragment is composed of a tandem repeat of two antiparallel four-helix bundles of virtually identical architectures that are related in structure to the dimerization domain of alpha-catenin and the tail region of vinculin. These results suggest that alpha-catenin is composed of repeating antiparallel helical domains. The region of alpha-catenin previously defined as an adhesion modulation domain corresponds to the C-terminal four-helix bundle of the M-fragment, and in the crystal lattice these domains exist as dimers. Evidence for dimerization of the M-fragment of alpha-catenin in solution was detected by chemical cross-linking experiments. The tendency of the adhesion modulation domain to form dimers may explain its biological activity of promoting cell-cell adhesiveness by inducing lateral dimerization of the associated cadherin molecule.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11447106}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11447106 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11447106}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Alpha-catenin]]
[[Category: Alpha-catenin]]
[[Category: Cytoskeleton]]
[[Category: Cytoskeleton]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:29:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:42:10 2008''

Revision as of 03:42, 1 July 2008

Image:1h6g.png

Template:STRUCTURE 1h6g

ALPHA-CATENIN M-DOMAIN

Template:ABSTRACT PUBMED 11447106

About this Structure

1H6G is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the M-fragment of alpha-catenin: implications for modulation of cell adhesion., Yang J, Dokurno P, Tonks NK, Barford D, EMBO J. 2001 Jul 16;20(14):3645-56. PMID:11447106

Page seeded by OCA on Tue Jul 1 06:42:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h6g"
Personal tools