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.


1und

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1und.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1und.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1und| PDB=1und | SCENE= }}
{{STRUCTURE_1und| PDB=1und | SCENE= }}
-
'''SOLUTION STRUCTURE OF THE HUMAN ADVILLIN C-TERMINAL HEADPIECE SUBDOMAIN'''
+
===SOLUTION STRUCTURE OF THE HUMAN ADVILLIN C-TERMINAL HEADPIECE SUBDOMAIN===
-
==Overview==
+
<!--
-
Headpiece (HP) is a 76-residue F-actin-binding module at the C terminus of many cytoskeletal proteins. Its 35-residue C-terminal subdomain is one of the smallest known motifs capable of autonomously adopting a stable, folded structure in the absence of any disulfide bridges, metal ligands, or unnatural amino acids. We report the three-dimensional solution structures of the C-terminal headpiece subdomains of human villin (HVcHP) and human advillin (HAcHP), determined by two-dimensional 1H-NMR. They represent the second and third structures of such C-terminal headpiece subdomains to be elucidated so far. A comparison with the structure of the chicken villin C-terminal subdomain reveals a high structural conservation. Both C-terminal subdomains bind specifically to F-actin. Mutagenesis is used to demonstrate the involvement of Trp 64 in the F-actin-binding surface. The latter residue is part of a conserved structural feature, in which the surface-exposed indole ring is stacked on the proline and lysine side chain embedded in a PXWK sequence motif. On the basis of the structural and mutational data concerning Trp 64 reported here, the results of a cysteine-scanning mutagenesis study of full headpiece, and a phage display mutational study of the 69-74 fragment, we propose a modification of the model, elaborated by Vardar and coworkers, for the binding of headpiece to F-actin.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15096633}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15096633 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15096633}}
==About this Structure==
==About this Structure==
-
1UND is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UND OCA].
+
1UND is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UND OCA].
==Reference==
==Reference==
Line 32: Line 36:
[[Category: F-actin binding]]
[[Category: F-actin binding]]
[[Category: Headpiece subdomain]]
[[Category: Headpiece subdomain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:27:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:09:22 2008''

Revision as of 03:09, 29 July 2008

Image:1und.png

Template:STRUCTURE 1und

SOLUTION STRUCTURE OF THE HUMAN ADVILLIN C-TERMINAL HEADPIECE SUBDOMAIN

Template:ABSTRACT PUBMED 15096633

About this Structure

1UND is a Single protein structure. Full experimental information is available from OCA.

Reference

Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements., Vermeulen W, Vanhaesebrouck P, Van Troys M, Verschueren M, Fant F, Goethals M, Ampe C, Martins JC, Borremans FA, Protein Sci. 2004 May;13(5):1276-87. PMID:15096633

Page seeded by OCA on Tue Jul 29 06:09:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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