2d2q
From Proteopedia
(New page: 200px<br /><applet load="2d2q" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d2q, resolution 2.8Å" /> '''Crystal structure of ...) |
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| - | [[Image:2d2q.gif|left|200px]]<br /><applet load="2d2q" size=" | + | [[Image:2d2q.gif|left|200px]]<br /><applet load="2d2q" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2d2q, resolution 2.8Å" /> | caption="2d2q, resolution 2.8Å" /> | ||
'''Crystal structure of the dimerized radixin FERM domain'''<br /> | '''Crystal structure of the dimerized radixin FERM domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ERM (ezrin/radixin/moesin) proteins bind to the cytoplasmic tail of | + | ERM (ezrin/radixin/moesin) proteins bind to the cytoplasmic tail of adhesion molecules in the formation of the membrane-associated cytoskeleton. The binding site is located in the FERM (4.1 and ERM) domain, a domain that is masked in the inactive form. A conventional masking motif, strand 1 (residues 494-500 in radixin), has previously been identified in the C-terminal tail domain. Here, the crystal structure of dimerized radixin FERM domains (residues 1-310) is presented in which the binding site of one molecule is occupied by the C-terminal residues (residues 295-304, strand 2) of the other molecule. The residues contain a conserved motif that is compatible with that identified in the adhesion molecules. The residues might serve as a second masking region in the inactive form of ERM proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 2D2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 2D2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2Q OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304., Kitano K, Yusa F, Hakoshima T, Acta | + | Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304., Kitano K, Yusa F, Hakoshima T, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):340-5. Epub 2006 Mar 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16582480 16582480] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: masking]] | [[Category: masking]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:47 2008'' |
Revision as of 14:54, 21 February 2008
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Crystal structure of the dimerized radixin FERM domain
Overview
ERM (ezrin/radixin/moesin) proteins bind to the cytoplasmic tail of adhesion molecules in the formation of the membrane-associated cytoskeleton. The binding site is located in the FERM (4.1 and ERM) domain, a domain that is masked in the inactive form. A conventional masking motif, strand 1 (residues 494-500 in radixin), has previously been identified in the C-terminal tail domain. Here, the crystal structure of dimerized radixin FERM domains (residues 1-310) is presented in which the binding site of one molecule is occupied by the C-terminal residues (residues 295-304, strand 2) of the other molecule. The residues contain a conserved motif that is compatible with that identified in the adhesion molecules. The residues might serve as a second masking region in the inactive form of ERM proteins.
About this Structure
2D2Q is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304., Kitano K, Yusa F, Hakoshima T, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):340-5. Epub 2006 Mar 25. PMID:16582480
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