1e5w: Difference between revisions

Revision as of 13:24, 21 February 2008

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

Page seeded by OCA on Thu Feb 21 12:24:10 2008

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OCA

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 '''STRUCTURE OF ISOLATED FERM DOMAIN AND FIRST LONG HELIX OF MOESIN'''<br />
 ==Overview==
-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.
+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 Structure==
-E5W 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E5W OCA].
+E5W 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=1E5W OCA].
 ==Reference==
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 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Edwards, S.D.]]
+[[Category: Edwards, S D.]]
-[[Category: Keep, N.H.]]
+[[Category: Keep, N H.]]
 [[Category: erm]]
 [[Category: ferm]]
 [[Category: moesin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:40:04 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:10 2008''