1olz | pdb_00001olz

THE LIGAND-BINDING FACE OF THE SEMAPHORINS REVEALED BY THE HIGH RESOLUTION CRYSTAL STRUCTURE OF SEMA4D

File:1olz.jpg

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Overview

Semaphorins, proteins characterized by an extracellular sema domain, regulate axon guidance, immune function and angiogenesis. The crystal, structure of SEMA4D (residues 1-657) shows the sema topology to be a, seven-bladed beta-propeller, revealing an unexpected homology with, integrins. The sema beta-propeller contains a distinctive 77-residue, insertion between beta-strands C and D of blade 5. Blade 7 is followed by, a domain common to plexins, semaphorins and integrins (PSI domain), which, forms a compact cysteine knot abutting the side of the propeller, and an, Ig-like domain. The top face of the beta-propeller presents prominent, loops characteristic of semaphorins. In addition to limited contact, between the Ig-like domains, the homodimer is stabilized through extensive, interactions between the top faces in a sector of the beta-propeller used, for heterodimerization in integrins. This face of the propeller also, mediates ligand binding in integrins, and functional data for, semaphorin-receptor interactions map to the equivalent surface.

About this Structure

1OLZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D., Love CA, Harlos K, Mavaddat N, Davis SJ, Stuart DI, Jones EY, Esnouf RM, Nat Struct Biol. 2003 Oct;10(10):843-8. Epub 2003 Sep 7. PMID:12958590

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