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.


1vyv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vyv.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1vyv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vyv| PDB=1vyv | SCENE= }}
{{STRUCTURE_1vyv| PDB=1vyv | SCENE= }}
-
'''BETA4 SUBUNIT OF CA2+ CHANNEL'''
+
===BETA4 SUBUNIT OF CA2+ CHANNEL===
-
==Overview==
+
<!--
-
High-voltage-activated Ca2+ channels are essential for diverse biological processes. They are composed of four or five subunits, including alpha1, alpha2-delta, beta and gamma (ref. 1). Their expression and function are critically dependent on the beta-subunit, which transports alpha1 to the surface membrane and regulates diverse channel properties. It is believed that the beta-subunit interacts with alpha1 primarily through the beta-interaction domain (BID), which binds directly to the alpha-interaction domain (AID) of alpha1; however, the molecular mechanism of the alpha1-beta interaction is largely unclear. Here we report the crystal structures of the conserved core region of beta3, alone and in complex with AID, and of beta4 alone. The structures show that the beta-subunit core contains two interacting domains: a Src homology 3 (SH3) domain and a guanylate kinase (GK) domain. The AID binds to a hydrophobic groove in the GK domain through extensive interactions, conferring extremely high affinity between alpha1 and beta-subunits. The BID is essential both for the structural integrity of and for bridging the SH3 and GK domains, but it does not participate directly in binding alpha1. The presence of multiple protein-interacting modules in the beta-subunit opens a new dimension to its function as a multi-functional protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15170217}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15170217 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15170217}}
==About this Structure==
==About this Structure==
Line 38: Line 42:
[[Category: Sh3 domain]]
[[Category: Sh3 domain]]
[[Category: Voltage-gated channel]]
[[Category: Voltage-gated channel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:55:43 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:53:18 2008''

Revision as of 16:53, 27 July 2008

Image:1vyv.png

Template:STRUCTURE 1vyv

BETA4 SUBUNIT OF CA2+ CHANNEL

Template:ABSTRACT PUBMED 15170217

About this Structure

1VYV is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structural basis of the alpha1-beta subunit interaction of voltage-gated Ca2+ channels., Chen YH, Li MH, Zhang Y, He LL, Yamada Y, Fitzmaurice A, Shen Y, Zhang H, Tong L, Yang J, Nature. 2004 Jun 10;429(6992):675-80. Epub 2004 May 30. PMID:15170217

Page seeded by OCA on Sun Jul 27 19:53:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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