The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization.

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