1B4F

OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN

Summary for 1B4F

Entry DOI	10.2210/pdb1b4f/pdb
Descriptor	EPHB2 (2 entities in total)
Functional Keywords	sam domain, eph receptor, signal transduction, oligomer
Biological source	Homo sapiens (human)
Total number of polymer chains	8
Total formula weight	75214.18
Authors	Thanos, C.D.,Goodwill, K.E.,Bowie, J.U. (deposition date: 1998-12-20, release date: 1999-02-16, Last modification date: 2024-02-07)
Primary citation	Thanos, C.D.,Goodwill, K.E.,Bowie, J.U. Oligomeric structure of the human EphB2 receptor SAM domain. Science, 283:833-836, 1999 Cited by PubMed Abstract: 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. PubMed: 9933164 DOI: 10.1126/science.283.5403.833 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.95 Å)

Structure validation