1KEX

Crystal Structure of the b1 Domain of Human Neuropilin-1

1KEX の概要

• エントリーDOI: 10.2210/pdb1kex/pdb
• 分子名称: Neuropilin-1 (2 entities in total)
• 機能のキーワード: beta barrel, jelly-roll, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: O14786
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17590.90

構造登録者

Lee, C.C.,Kreusch, A.,McMullan, D.,Ng, K.,Spraggon, G. (登録日: 2001-11-18, 公開日: 2003-01-28, 最終更新日: 2024-11-20)

主引用文献

Lee, C.C.,Kreusch, A.,McMullan, D.,Ng, K.,Spraggon, G.
Crystal Structure of the Human Neuropilin-1 b1 Domain
Structure, 11:99-108, 2003

PubMed Abstract: 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.

PubMed: 12517344
DOI: 10.1016/S0969-2126(02)00941-3

実験手法

X-RAY DIFFRACTION (1.9 Å)