1gp9

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Revision as of 15:01, 12 November 2007

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spinqualitylabelsall models 1gp9, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

A NEW CRYSTAL FORM OF THE NK1 SPLICE VARIANT OF HGF/SF DEMONSTRATES EXTENSIVE HINGE MOVEMENT AND SUGGESTS THAT THE NK1 DIMER ORIGINATES BY DOMAIN SWAPPING

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

NK1 is a splice variant of the polypeptide growth factor HGF/SF that, consists of the N terminal (N) and first kringle (K) domains and retains, receptor binding and signalling. While NK1 behaves as a monomer in, solution, two independent crystallographic structures have previously, shown an identical, tightly packed dimer. Here we report a novel, orthorhombic crystal form of NK1 at 2.5 A resolution in which four NK1, protomers are packed in two distinct dimers in the asymmetric unit., Although the basic architecture of the new NK1 dimers is similar to the, two described earlier, the new crystal form demonstrates extensive hinge, movement between the N and K domain that leads to re-orientation of the, receptor-binding sites. The hinge bending is evidence of the paucity of, strong interactions between domains within the protomer, in contrast to, the extensive interactions between protomers in the dimer. These, observations are consistent with domain swapping in the dimer, such that, the interdomain interactions of the monomer are replaced by equivalent, interprotomer interactions in the dimer and offer a route for protein, engineering of NK1 variants which may act as receptor antagonists.

Disease

Known diseases associated with this structure: Fibromatosis, gingival OMIM:[182530], Noonan syndrome 4 OMIM:[182530]

About this Structure

1GP9 is a Single protein structure of sequence from Homo sapiens with EPE as ligand. Full crystallographic information is available from OCA.

Reference

A new crystal form of the NK1 splice variant of HGF/SF demonstrates extensive hinge movement and suggests that the NK1 dimer originates by domain swapping., Watanabe K, Chirgadze DY, Lietha D, de Jonge H, Blundell TL, Gherardi E, J Mol Biol. 2002 May 31;319(2):283-8. PMID:12051906

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