1jpa
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Crystal Structure of unphosphorylated EphB2 receptor tyrosine kinase and juxtamembrane region
OverviewOverview
The Eph receptor tyrosine kinase family is regulated by, autophosphorylation within the juxtamembrane region and the kinase, activation segment. We have solved the X-ray crystal structure to 1.9 A, resolution of an autoinhibited, unphosphorylated form of EphB2 comprised, of the juxtamembrane region and the kinase domain. The structure, supported by mutagenesis data, reveals that the juxtamembrane segment, adopts a helical conformation that distorts the small lobe of the kinase, domain, and blocks the activation segment from attaining an activated, conformation. Phosphorylation of conserved juxtamembrane tyrosines would, relieve this autoinhibition by disturbing the association of the, juxtamembrane segment with the kinase domain, while liberating, phosphotyrosine sites for binding SH2 domains of target proteins. We, propose that the autoinhibitory mechanism employed by EphB2 is a more, general device through which receptor tyrosine kinases are controlled.
About this StructureAbout this Structure
1JPA is a Single protein structure of sequence from Mus musculus with ANP as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region., Wybenga-Groot LE, Baskin B, Ong SH, Tong J, Pawson T, Sicheri F, Cell. 2001 Sep 21;106(6):745-57. PMID:11572780
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