1e5w: Difference between revisions
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[[Image:1e5w.gif|left|200px]] | [[Image:1e5w.gif|left|200px]] | ||
'''STRUCTURE OF ISOLATED FERM DOMAIN AND FIRST LONG HELIX OF MOESIN''' | {{Structure | ||
|PDB= 1e5w |SIZE=350|CAPTION= <scene name='initialview01'>1e5w</scene>, resolution 2.70Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF ISOLATED FERM DOMAIN AND FIRST LONG HELIX OF MOESIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E5W is a [ | 1E5W is a [[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=1E5W OCA]. | ||
==Reference== | ==Reference== | ||
The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation., Edwards SD, Keep NH, Biochemistry. 2001 Jun 19;40(24):7061-8. PMID:[http:// | The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation., Edwards SD, Keep NH, Biochemistry. 2001 Jun 19;40(24):7061-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11401550 11401550] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: moesin]] | [[Category: moesin]] | ||
''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 10:50:14 2008'' | ||
Revision as of 11:50, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF ISOLATED FERM DOMAIN AND FIRST LONG HELIX OF MOESIN
OverviewOverview
Moesin binds to a large range of proteins through its N terminal FERM (band 4.1, ezrin, radixin, moesin) domain. In full-length moesin isolated from cells, this binding is masked by binding to the C-terminal domain of moesin (C-ERMAD). Activation takes place by phosphorylation of Thr 558 in the C-ERMAD, which releases the C-ERMAD. A recently determined crystal structure of a noncovalent complex of the FERM and C-ERMAD domains showed for the first time that the structure of the FERM domain consists of three subdomains, each of which is similar to known structures. The structure reported here also contains a unique 47-residue helix pointing away from the FERM domain at the start of the alpha domain, in agreement with secondary structure predictions. Removal of the C-ERMAD does not result in a huge rearrangement of the FERM domain, but comparison with the activated radixin structure shows a consistent set of small changes. Not surprisingly, the exposed C-ERMAD binding area interacts in crystal contacts. More interestingly, a negatively charged peptide binds to the inositol site in a crystal contact and causes a greater conformational change in the structure than inositol.
About this StructureAbout this Structure
1E5W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation., Edwards SD, Keep NH, Biochemistry. 2001 Jun 19;40(24):7061-8. PMID:11401550
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