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2d2q
From Proteopedia
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| - | [[Image:2d2q.gif|left|200px]] | + | [[Image:2d2q.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of the dimerized radixin FERM domain''' | + | {{Structure |
| + | |PDB= 2d2q |SIZE=350|CAPTION= <scene name='initialview01'>2d2q</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the dimerized radixin FERM domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2D2Q is a [ | + | 2D2Q is a [[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 Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):340-5. Epub 2006 Mar 25. PMID:[http:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/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://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:22:36 2008'' |
Revision as of 14:22, 20 March 2008
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| , resolution 2.8Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 16:22:36 2008
