1sgh: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:1sgh.gif|left|200px]]
{{Seed}}
[[Image:1sgh.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sgh|  PDB=1sgh  |  SCENE=  }}  
{{STRUCTURE_1sgh|  PDB=1sgh  |  SCENE=  }}  


'''Moesin FERM domain bound to EBP50 C-terminal peptide'''
===Moesin FERM domain bound to EBP50 C-terminal peptide===




==Overview==
<!--  
Members of the ezrin-radixin-moesin (ERM) protein family serve as regulated microfilament-membrane crosslinking proteins that, upon activation, bind the scaffolding protein ERM-phosphoprotein of 50 kDa (EBP50). Here we report a 3.5 A resolution diffraction analysis of a complex between the active moesin N-terminal FERM domain and a 38 residue peptide from the C terminus of EBP50. This crystallographic result, combined with sequence and structural comparisons, suggests that the C-terminal 11 residues of EBP50 binds as an alpha-helix at the same site occupied in the dormant monomer by the last 11 residues of the inhibitory moesin C-terminal tail. Biochemical support for this interpretation derives from in vitro studies showing that appropriate mutations in both the EBP50 tail peptide and the FERM domain reduce binding, and that a peptide representing just the C-terminal 14 residues of EBP50 also binds to moesin. Combined with the recent identification of the I-CAM-2 binding site on the ERM FERM domain (Hamada, K., Shimizu, T., Yonemura, S., Tsukita, S., and Hakoshima, T. (2003) EMBO J. 22, 502-514), this study reveals that the FERM domain contains two distinct binding sites for membrane-associated proteins. The contribution of each ligand to ERM function can now be dissected by making structure-based mutations that specifically affect the binding of each ligand.
The line below this paragraph, {{ABSTRACT_PUBMED_15020681}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15020681 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15020681}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Karplus, P A.]]
[[Category: Karplus, P A.]]
[[Category: Ferm-peptide complex]]
[[Category: Ferm-peptide complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:40:17 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:59:45 2008''

Revision as of 05:59, 29 July 2008

File:1sgh.png

Template:STRUCTURE 1sgh

Moesin FERM domain bound to EBP50 C-terminal peptide

Template:ABSTRACT PUBMED 15020681

About this Structure

1SGH is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain., Finnerty CM, Chambers D, Ingraffea J, Faber HR, Karplus PA, Bretscher A, J Cell Sci. 2004 Mar 15;117(Pt 8):1547-52. PMID:15020681

Page seeded by OCA on Tue Jul 29 08:59:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1sgh&oldid=735647"