1nuk
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1nuk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nuk, resolution 2.9Å" /> '''CRYSTAL STRUCTURE OF ...)
Next diff →
Revision as of 20:26, 20 November 2007
|
CRYSTAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE EPHB2 RECEPTOR TYROSINE KINASE
Overview
The Eph receptors, which bind a group of cell-membrane-anchored ligands, known as ephrins, represent the largest subfamily of receptor tyrosine, kinases (RTKs). They are predominantly expressed in the developing and, adult nervous system and are important in contact-mediated axon guidance, axon fasciculation and cell migration. Eph receptors are unique among, other RTKs in that they fall into two subclasses with distinct ligand, specificities, and in that they can themselves function as ligands to, activate bidirectional cell-cell signalling. We report here the crystal, structure at 2.9 A resolution of the amino-terminal ligand-binding domain, of the EphB2 receptor (also known as Nuk). The domain folds into a compact, jellyroll beta-sandwich composed of 11 antiparallel beta-strands. Using, structure-based mutagenesis, we have identified an extended loop that is, important for ligand binding and class specificity. This loop, which is, conserved within but not between Eph RTK subclasses, packs against the, concave beta-sandwich surface near positions at which missense mutations, cause signalling defects, localizing the ligand-binding region on the, surface of the receptor.
About this Structure
1NUK is a Single protein structure of sequence from Mus musculus. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2., Himanen JP, Henkemeyer M, Nikolov DB, Nature. 1998 Dec 3;396(6710):486-91. PMID:9853759
Page seeded by OCA on Tue Nov 20 22:34:02 2007
