1b0x

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[[Image:1b0x.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b0x OCA], [http://www.ebi.ac.uk/pdbsum/1b0x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b0x RCSB]</span>
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'''THE CRYSTAL STRUCTURE OF AN EPH RECEPTOR SAM DOMAIN REVEALS A MECHANISM FOR MODULAR DIMERIZATION.'''
'''THE CRYSTAL STRUCTURE OF AN EPH RECEPTOR SAM DOMAIN REVEALS A MECHANISM FOR MODULAR DIMERIZATION.'''
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[[Category: Sicheri, F.]]
[[Category: Sicheri, F.]]
[[Category: Stapleton, D.]]
[[Category: Stapleton, D.]]
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[[Category: dimerization domain]]
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[[Category: Dimerization domain]]
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[[Category: protein interaction module]]
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[[Category: Protein interaction module]]
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[[Category: receptor tyrosine kinase]]
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[[Category: Receptor tyrosine kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:56:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:51:27 2008''
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Revision as of 07:56, 2 May 2008

Template:STRUCTURE 1b0x

THE CRYSTAL STRUCTURE OF AN EPH RECEPTOR SAM DOMAIN REVEALS A MECHANISM FOR MODULAR DIMERIZATION.


Overview

The sterile alpha motif (SAM) domain is a novel protein module of approximately 70 amino acids that is found in a variety of signaling molecules including tyrosine and serine/threonine protein kinases, cytoplasmic scaffolding and adaptor proteins, regulators of lipid metabolism, and GTPases as well as members of the ETS family of transcription factors. The SAM domain can potentially function as a protein interaction module through the ability to homo- and hetero-oligomerize with other SAM domains. This functional property elicits the oncogenic activation of chimeric proteins arising from translocation of the SAM domain of TEL to coding regions of the betaPDGF receptor, Abl, JAK2 protein kinase and the AML1 transcription factor. Here we describe the 2.0 A X-ray crystal structure of a SAM domain homodimer from the intracellular region of the EphA4 receptor tyrosine kinase. The structure reveals a mode of dimerization that we predict is shared amongst the SAM domains of the Eph receptor tyrosine kinases and possibly other SAM domain containing proteins. These data indicate a mechanism through which an independently folding protein module can form homophilic complexes that regulate signaling events at the membrane and in the nucleus.

About this Structure

1B0X is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization., Stapleton D, Balan I, Pawson T, Sicheri F, Nat Struct Biol. 1999 Jan;6(1):44-9. PMID:9886291 Page seeded by OCA on Fri May 2 10:56:15 2008

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