1v05

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{{STRUCTURE_1v05| PDB=1v05 | SCENE= }}
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'''DIMERIZATION OF HUMAN FILAMIN C: CRYSTAL STRUCTURE OF THE DOMAIN 24'''
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===DIMERIZATION OF HUMAN FILAMIN C: CRYSTAL STRUCTURE OF THE DOMAIN 24===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15642266}}
==About this Structure==
==About this Structure==
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[[Category: Actin-binding protein]]
[[Category: Actin-binding protein]]
[[Category: Immunoglobulin]]
[[Category: Immunoglobulin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:55:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:40:53 2008''

Revision as of 11:40, 28 July 2008

Image:1v05.png


PDB ID 1v05

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1v05, resolution 1.43Å ()
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



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

Template:ABSTRACT PUBMED 15642266

About this Structure

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

Reference

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

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