1b4f

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{{STRUCTURE_1b4f| PDB=1b4f | SCENE= }}
{{STRUCTURE_1b4f| PDB=1b4f | SCENE= }}
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'''OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN'''
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===OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 9933164 is the PubMed ID number.
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:03:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:13:48 2008''

Revision as of 15:13, 30 June 2008

Template:STRUCTURE 1b4f

OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN

Template:ABSTRACT PUBMED 9933164

About this Structure

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

Reference

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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