1kex | pdb_00001kex
Crystal Structure of the b1 Domain of Human Neuropilin-1
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Overview
Neuropilin-1 (Npn-1) is a type I cell surface receptor involved in a broad, range of developmental processes, including axon guidance, angiogenesis, and heterophilic cell adhesion. We have determined the crystal structure, of the human Npn-1 b1 domain to 1.9 A. The overall structure resembles, coagulation factor V and VIII (F5/8) C1 and C2 domains, exhibiting a, distorted jellyroll fold. Details of the structure provide insight to b1, domain regions responsible for ligand binding and facilitate, rationalization of existing biochemical binding data. A polar cleft formed, by adjacent loops at one end of the molecule in conjunction with flanking, electronegative surfaces may represent the binding site for the positively, charged tails of semaphorins and VEGF(165). The nature of the cell, adhesion binding site of the b1 domain can be visualized in context of the, structure.
Disease
Known diseases associated with this structure: Glaucoma 1, open angle, E OMIM:[602432], Glaucoma, normal tension, susceptibility to OMIM:[602432]
About this Structure
1KEX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human neuropilin-1 b1 domain., Lee CC, Kreusch A, McMullan D, Ng K, Spraggon G, Structure. 2003 Jan;11(1):99-108. PMID:12517344
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