1b4f
From Proteopedia
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'''OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN''' | '''OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN''' | ||
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[[Category: Goodwill, K E.]] | [[Category: Goodwill, K E.]] | ||
[[Category: Thanos, C D.]] | [[Category: Thanos, C D.]] | ||
- | [[Category: | + | [[Category: Eph receptor]] |
- | [[Category: | + | [[Category: Oligomer]] |
- | [[Category: | + | [[Category: Sam domain]] |
- | [[Category: | + | [[Category: Signal transduction]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:03:19 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 08:03, 2 May 2008
OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN
Overview
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.
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 Page seeded by OCA on Fri May 2 11:03:19 2008