2emt: Difference between revisions

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[[Image:2emt.jpg|left|200px]]
[[Image:2emt.jpg|left|200px]]


{{Structure
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{{STRUCTURE_2emt|  PDB=2emt |  SCENE= }}  
|RELATEDENTRY=[[1j19|1J19]], [[1gc6|1GC6]], [[1gc7|1GC7]], [[2d11|2D11]], [[2d10|2D10]], [[2d2q|2D2Q]], [[2ems|2EMS]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2emt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2emt OCA], [http://www.ebi.ac.uk/pdbsum/2emt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2emt RCSB]</span>
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'''Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1'''
'''Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1'''
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[[Category: Takai, Y.]]
[[Category: Takai, Y.]]
[[Category: Terawaki, S.]]
[[Category: Terawaki, S.]]
[[Category: cell adhesion]]
[[Category: Cell adhesion]]
[[Category: protein-peptide complex]]
[[Category: Protein-peptide complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 02:48:12 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:51:13 2008''

Revision as of 23:48, 3 May 2008

File:2emt.jpg

Template:STRUCTURE 2emt

Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1


Overview

P-selectin glycoprotein ligand-1 (PSGL-1), an adhesion molecule with O-glycosylated extracellular sialomucins, is involved in leukocyte inflammatory responses. On activation, ezrin-radixin-moesin (ERM) proteins mediate the redistribution of PSGL-1 on polarized cell surfaces to facilitate binding to target molecules. ERM proteins recognize a short binding motif, Motif-1, conserved in cytoplasmic tails of adhesion molecules, whereas PSGL-1 lacks Motif-1 residues important for binding to ERM proteins. The crystal structure of the complex between the radixin FERM domain and a PSGL-1 juxtamembrane peptide reveals that the peptide binds the groove of FERM subdomain C by forming a beta-strand associated with strand beta5C, followed by a loop flipped out towards the solvent. The Motif-1 3(10) helix present in the FERM-ICAM-2 complex is absent in PSGL-1 given the absence of a critical Motif-1 alanine residue, and PSGL-1 reduces its contact area with subdomain C. Non-conserved positions are occupied by large residues Met9 and His8, which stabilize peptide conformation and enhance groove binding. Non-conserved residues play an important role in compensating for loss of binding energy resulting from the absence of conserved residues important for binding.

About this Structure

2EMT is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural basis of PSGL-1 binding to ERM proteins., Takai Y, Kitano K, Terawaki S, Maesaki R, Hakoshima T, Genes Cells. 2007 Dec;12(12):1329-38. PMID:18076570 Page seeded by OCA on Sun May 4 02:48:12 2008

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