Publication Date:
1999-02-05
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thanos, C D -- Goodwill, K E -- Bowie, J U -- New York, N.Y. -- Science. 1999 Feb 5;283(5403):833-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UCLA-DOE Laboratory of Structural Biology and Molecular Medicine and Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9933164" target="_blank"〉PubMed〈/a〉
Keywords:
Binding Sites
;
Crystallization
;
Crystallography, X-Ray
;
Dimerization
;
GRB10 Adaptor Protein
;
Humans
;
Hydrogen Bonding
;
Kinesin/metabolism
;
Models, Molecular
;
Myosins/metabolism
;
Phosphorylation
;
*Protein Conformation
;
Protein Structure, Secondary
;
Protein Tyrosine Phosphatases/metabolism
;
Proteins/metabolism
;
Receptor Aggregation
;
Receptor Protein-Tyrosine Kinases/*chemistry/metabolism
;
Receptor, EphB2
;
Recombinant Proteins/chemistry/metabolism
;
Surface Properties
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
