2emt: Difference between revisions

Revision as of 21:07, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2emt.png

Template:STRUCTURE 2emt

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

Template:ABSTRACT PUBMED 18076570

About this StructureAbout this Structure

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

ReferenceReference

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

Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1., Takai Y, Kitano K, Terawaki S, Maesaki R, Hakoshima T, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt, 1):49-51. Epub 2006 Dec 22. PMID:17183174

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2emt|  PDB=2emt  |  SCENE=  }}
-'''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===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18076570}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18076570 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18076570}}
 ==About this Structure==
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 ==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:[http://www.ncbi.nlm.nih.gov/pubmed/18076570 18076570]
+Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1., Takai Y, Kitano K, Terawaki S, Maesaki R, Hakoshima T, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt, 1):49-51. Epub 2006 Dec 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17183174 17183174]
 [[Category: Mus musculus]]
 [[Category: Protein complex]]
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 [[Category: Cell adhesion]]
 [[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 Sun Jul 27 21:07:18 2008''