1b4f: Difference between revisions

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{{STRUCTURE_1b4f|  PDB=1b4f  |  SCENE=  }}  
{{STRUCTURE_1b4f|  PDB=1b4f  |  SCENE=  }}  


'''OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN'''
===OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN===




==Overview==
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The sterile alpha motif (SAM) domain is a protein interaction module that is present in diverse signal-transducing proteins. SAM domains are known to form homo- and hetero-oligomers. The crystal structure of the SAM domain from an Eph receptor tyrosine kinase, EphB2, reveals two large interfaces. In one interface, adjacent monomers exchange amino-terminal peptides that insert into a hydrophobic groove on each neighbor. A second interface is composed of the carboxyl-terminal helix and a nearby loop. A possible oligomer, constructed from a combination of these binding modes, may provide a platform for the formation of larger protein complexes.
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{{ABSTRACT_PUBMED_9933164}}


==About this Structure==
==About this Structure==
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[[Category: Sam domain]]
[[Category: Sam domain]]
[[Category: Signal transduction]]
[[Category: Signal transduction]]
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Revision as of 18:13, 30 June 2008

File:1b4f.png

Template:STRUCTURE 1b4f

OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAINOLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN

Template:ABSTRACT PUBMED 9933164

About this StructureAbout this Structure

1B4F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Oligomeric structure of the human EphB2 receptor SAM domain., Thanos CD, Goodwill KE, Bowie JU, Science. 1999 Feb 5;283(5403):833-6. PMID:9933164

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