This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1kex
From Proteopedia
Revision as of 11:19, 28 September 2014 by OCA (Talk | contribs)
1kex is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Lee CC, Kreusch A, McMullan D, Ng K, Spraggon G. Crystal structure of the human neuropilin-1 b1 domain. Structure. 2003 Jan;11(1):99-108. PMID:12517344
