2QQM
Crystal Structure of the a2b1b2 Domains from Human Neuropilin-1
Summary for 2QQM
| Entry DOI | 10.2210/pdb2qqm/pdb |
| Related | 2QQI 2QQJ 2QQK 2QQL 2QQN 2QQO |
| Descriptor | Neuropilin-1, alpha-L-fucopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | vegf receptor, semaphorin receptor, calcium-binding domain, angiogenesis, developmental protein, differentiation, glycoprotein, heparan sulfate, membrane, neurogenesis, proteoglycan, secreted, transmembrane, hormone, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 52297.82 |
| Authors | Appleton, B.A.,Wiesmann, C. (deposition date: 2007-07-26, release date: 2007-11-20, Last modification date: 2024-11-20) |
| Primary citation | Appleton, B.A.,Wu, P.,Maloney, J.,Yin, J.,Liang, W.C.,Stawicki, S.,Mortara, K.,Bowman, K.K.,Elliott, J.M.,Desmarais, W.,Bazan, J.F.,Bagri, A.,Tessier-Lavigne, M.,Koch, A.W.,Wu, Y.,Watts, R.J.,Wiesmann, C. Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding Embo J., 26:4902-4912, 2007 Cited by PubMed Abstract: Neuropilins (Nrps) are co-receptors for class 3 semaphorins and vascular endothelial growth factors and important for the development of the nervous system and the vasculature. The extracellular portion of Nrp is composed of two domains that are essential for semaphorin binding (a1a2), two domains necessary for VEGF binding (b1b2), and one domain critical for receptor dimerization (c). We report several crystal structures of Nrp1 and Nrp2 fragments alone and in complex with antibodies that selectively block either semaphorin or vascular endothelial growth factor (VEGF) binding. In these structures, Nrps adopt an unexpected domain arrangement in which the a2, b1, and b2 domains form a tightly packed core that is only loosely connected to the a1 domain. The locations of the antibody epitopes together with in vitro experiments indicate that VEGF and semaphorin do not directly compete for Nrp binding. Based upon our structural and functional data, we propose possible models for ligand binding to neuropilins. PubMed: 17989695DOI: 10.1038/sj.emboj.7601906 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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