1e5w: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1e5w.gif|left|200px]]
{{Seed}}
[[Image:1e5w.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e5w|  PDB=1e5w  |  SCENE=  }}  
{{STRUCTURE_1e5w|  PDB=1e5w  |  SCENE=  }}  


'''STRUCTURE OF ISOLATED FERM DOMAIN AND FIRST LONG HELIX OF MOESIN'''
===STRUCTURE OF ISOLATED FERM DOMAIN AND FIRST LONG HELIX OF MOESIN===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_11401550}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11401550 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11401550}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Ferm]]
[[Category: Ferm]]
[[Category: Moesin]]
[[Category: Moesin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:42:14 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:12:05 2008''

Revision as of 21:12, 30 June 2008

File:1e5w.png

Template:STRUCTURE 1e5w

STRUCTURE OF ISOLATED FERM DOMAIN AND FIRST LONG HELIX OF MOESIN

Template:ABSTRACT PUBMED 11401550

About this Structure

1E5W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

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:11401550

Page seeded by OCA on Tue Jul 1 00:12:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1e5w&oldid=590771"