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.


1qag

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qag.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1qag.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qag| PDB=1qag | SCENE= }}
{{STRUCTURE_1qag| PDB=1qag | SCENE= }}
-
'''Actin binding region of the dystrophin homologue utrophin'''
+
===Actin binding region of the dystrophin homologue utrophin===
-
==Overview==
+
<!--
-
BACKGROUND: Utrophin is a large multidomain protein that belongs to a superfamily of actin-binding proteins, which includes dystrophin, alpha-actinin, beta-spectrin, fimbrin, filamin and plectin. All the members of this family contain a common actin-binding region at their N termini and perform a wide variety of roles associated with the actin cytoskeleton. Utrophin is the autosomal homologue of dystrophin, the protein defective in the X-linked Duchenne and Becker muscular dystrophies, and upregulation of utrophin has been suggested as a potential therapy for muscular dystrophy patients. RESULTS: The structure of the actin-binding region of utrophin, consisting of two calponin-homology (CH) domains, has been solved at 3.0 A resolution. It is composed of an antiparallel dimer with each of the monomers being present in an extended dumbell shape and the two CH domains being separated by a long central helix. This extended conformation is in sharp contrast to the compact monomer structure of the N-terminal actin-binding region of fimbrin. CONCLUSIONS: The crystal structure of the actin-binding region of utrophin suggests that these actin-binding domains may be more flexible than was previously thought and that this flexibility may allow domain reorganisation and play a role in the actin-binding mechanism. Thus utrophin could possibly bind to actin in an extended conformation so that the sites previously identified as being important for actin binding may be directly involved in this interaction.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10647184}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10647184 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10647184}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Dystrophin]]
[[Category: Dystrophin]]
[[Category: Utrophin]]
[[Category: Utrophin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:03:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:46:19 2008''

Revision as of 16:46, 28 July 2008

Image:1qag.png

Template:STRUCTURE 1qag

Actin binding region of the dystrophin homologue utrophin

Template:ABSTRACT PUBMED 10647184

About this Structure

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

Reference

Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimer., Keep NH, Winder SJ, Moores CA, Walke S, Norwood FL, Kendrick-Jones J, Structure. 1999 Dec 15;7(12):1539-46. PMID:10647184

Page seeded by OCA on Mon Jul 28 19:46:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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