1b4f: Difference between revisions

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==Overview==
==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.
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.


==Disease==
==Disease==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bowie, J.U.]]
[[Category: Bowie, J U.]]
[[Category: Goodwill, K.E.]]
[[Category: Goodwill, K E.]]
[[Category: Thanos, C.D.]]
[[Category: Thanos, C D.]]
[[Category: eph receptor]]
[[Category: eph receptor]]
[[Category: oligomer]]
[[Category: oligomer]]
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[[Category: signal transduction]]
[[Category: signal transduction]]


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Revision as of 12:51, 21 February 2008

File:1b4f.jpg


1b4f, resolution 1.95Å

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OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN

OverviewOverview

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.

DiseaseDisease

Known diseases associated with this structure: Prostate cancer, progression and metastasis of OMIM:[600997]

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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