1b4f: Difference between revisions

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[[Image:1b4f.jpg|left|200px]]
{{Seed}}
[[Image:1b4f.png|left|200px]]


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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.
The line below this paragraph, {{ABSTRACT_PUBMED_9933164}}, adds the Publication Abstract to the page
(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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