1KEX
Crystal Structure of the b1 Domain of Human Neuropilin-1
Summary for 1KEX
| Entry DOI | 10.2210/pdb1kex/pdb |
| Descriptor | Neuropilin-1 (2 entities in total) |
| Functional Keywords | beta barrel, jelly-roll, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: O14786 |
| Total number of polymer chains | 1 |
| Total formula weight | 17590.90 |
| Authors | Lee, C.C.,Kreusch, A.,McMullan, D.,Ng, K.,Spraggon, G. (deposition date: 2001-11-18, release date: 2003-01-28, Last modification date: 2024-11-20) |
| Primary citation | 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 Cited by 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: 12517344DOI: 10.1016/S0969-2126(02)00941-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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