2emt

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{{STRUCTURE_2emt| PDB=2emt | SCENE= }}
{{STRUCTURE_2emt| PDB=2emt | SCENE= }}
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'''Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1'''
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===Crystal Structure Analysis of the radixin FERM domain complexed with adhesion molecule PSGL-1===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 18076570 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18076570}}
==About this Structure==
==About this Structure==
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==Reference==
==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]
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]
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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: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Cell adhesion]]
[[Category: Cell adhesion]]
[[Category: Protein-peptide complex]]
[[Category: Protein-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:48:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:07:18 2008''

Revision as of 18:07, 27 July 2008

Image:2emt.png

Template:STRUCTURE 2emt

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

Template:ABSTRACT PUBMED 18076570

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

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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