2QQM: Crystal Structure Of The A2b1b2 Domains From Human Neuropilin-1

Citation:
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.
PDB ID: 2QQMDownload
MMDB ID: 60817
PDB Deposition Date: 2007/7/26
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 2QQM: monomeric; determined by author and by software (PISA)
Molecular Components in 2QQM
Label Count Molecule
Protein (1 molecule)
1
Neuropilin-1(Gene symbol: NRP1)
Molecule annotation
Chemicals (13 molecules)
1
1
2
6
3
4
4
2
* Click molecule labels to explore molecular sequence information.

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