1v05
From Proteopedia
(New page: 200px<br /> <applet load="1v05" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v05, resolution 1.43Å" /> '''DIMERIZATION OF HUM...) |
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| - | [[Image:1v05.gif|left|200px]]<br /> | + | [[Image:1v05.gif|left|200px]]<br /><applet load="1v05" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1v05" size=" | + | |
caption="1v05, resolution 1.43Å" /> | caption="1v05, resolution 1.43Å" /> | ||
'''DIMERIZATION OF HUMAN FILAMIN C: CRYSTAL STRUCTURE OF THE DOMAIN 24'''<br /> | '''DIMERIZATION OF HUMAN FILAMIN C: CRYSTAL STRUCTURE OF THE DOMAIN 24'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Filamins are essential in cell motility and many developmental processes. | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1V05 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1V05 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V05 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Kiema, T | + | [[Category: Kiema, T R.]] |
[[Category: Pudas, R.]] | [[Category: Pudas, R.]] | ||
[[Category: Ylanne, J.]] | [[Category: Ylanne, J.]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:30:12 2008'' |
Revision as of 13:30, 21 February 2008
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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.
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
Page seeded by OCA on Thu Feb 21 15:30:12 2008
