1JPA
Crystal Structure of unphosphorylated EphB2 receptor tyrosine kinase and juxtamembrane region
Summary for 1JPA
| Entry DOI | 10.2210/pdb1jpa/pdb |
| Descriptor | neural kinase, Nuk=Eph/Elk/Eck family receptor-like tyrosine kinase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total) |
| Functional Keywords | receptor tyrosine kinase, autoinhibited, unphosphorylated, juxtamembrane, transferase |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Membrane; Single-pass type I membrane protein: P54763 |
| Total number of polymer chains | 2 |
| Total formula weight | 71661.32 |
| Authors | Wybenga-Groot, L.E.,Pawson, T.,Sicheri, F. (deposition date: 2001-08-01, release date: 2001-10-03, Last modification date: 2024-04-03) |
| Primary citation | Wybenga-Groot, L.E.,Baskin, B.,Ong, S.H.,Tong, J.,Pawson, T.,Sicheri, F. Structural basis for autoinhibition of the Ephb2 receptor tyrosine kinase by the unphosphorylated juxtamembrane region. Cell(Cambridge,Mass.), 106:745-757, 2001 Cited by PubMed Abstract: 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. PubMed: 11572780DOI: 10.1016/S0092-8674(01)00496-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.91 Å) |
Structure validation
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