1v05: Difference between revisions

Revision as of 14:40, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1v05.png

1v05, resolution 1.43Å ()

Structural annotation:
Resources:	CATH : 1V05A00 InterPro : Ipr001589, Ipr013783, Ipr001715, Ipr001298, Ipr014756 Pfam : PF00630 UniProt : Q14315

Functional annotation:
Cellular component:	actin cytoskeleton membrane cytoplasm cytoskeleton
Molecular function:	protein binding actin binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

DIMERIZATION OF HUMAN FILAMIN C: CRYSTAL STRUCTURE OF THE DOMAIN 24DIMERIZATION OF HUMAN FILAMIN C: CRYSTAL STRUCTURE OF THE DOMAIN 24

Template:ABSTRACT PUBMED 15642266

About this StructureAbout this Structure

1V05 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for vertebrate filamin dimerization., Pudas R, Kiema TR, Butler PJ, Stewart M, Ylanne J, Structure. 2005 Jan;13(1):111-9. PMID:15642266

Page seeded by OCA on Mon Jul 28 14:40:53 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''DIMERIZATION OF HUMAN FILAMIN C: CRYSTAL STRUCTURE OF THE DOMAIN 24'''
+===DIMERIZATION OF HUMAN FILAMIN C: CRYSTAL STRUCTURE OF THE DOMAIN 24===
-==Overview==
+<!--
-Filamins are essential in cell motility and many developmental processes. They are large actin cross linking proteins that contain actin binding domains in their N termini and a long rod region constructed from 24 tandem Ig domains. Dimerization is crucial for the actin crosslinking function of filamins and requires the most C-terminal Ig domain. We describe here the crystal structure of this 24th Ig domain (Ig24) of human filamin C and show how it mediates dimerization. The dimer interface is novel and quite different to that seen in the Dictyostelium discoideum filamin analog. The sequence signature of the dimerization interface suggests that the C-terminal domains of all vertebrate filamins share the same dimerization mechanism. Furthermore, we show that point mutations in the dimerization interface disrupt the dimer and that the dissociation constant for recombinant Ig24 is in the micromolar range.
+The line below this paragraph, {{ABSTRACT_PUBMED_15642266}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15642266}}
 ==About this Structure==
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 [[Category: Actin-binding protein]]
 [[Category: Immunoglobulin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:55:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:40:53 2008''