Sandbox Reserved 1658
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
- | <p align="justify"> | + | <p align="justify">Neuropilin-1 has three different domains. A cytoplasmic domain which contains 40 residues, a transmembrane domain which contains 24 residues and a 850-residues ectodomain. The latter is an assembly of five individual motifs (a1,a2,b1,b2 and c). It contains, hence two CUB domains (a1/a2), two homologous domains to coagulation factors V/VIII (b1/b2) and a MAM domain (c). The ligand binding is mediated by the (a1/a2) and (b1/b2) portion of the ectodomain while the c domain mediates Neuripilin oligomerization.</p> |
<p align="justify"> The semaphorins (SEMA) bind to the (a1/a2/b1) domains while Vascular endothelial growth factors (VEGFs) bind to (b1/b2). The c domain as well as the transmembrane domain, are involved in the receptor dimerization.</p> | <p align="justify"> The semaphorins (SEMA) bind to the (a1/a2/b1) domains while Vascular endothelial growth factors (VEGFs) bind to (b1/b2). The c domain as well as the transmembrane domain, are involved in the receptor dimerization.</p> |
Revision as of 11:55, 9 January 2021
This Sandbox is Reserved from 26/11/2020, through 26/11/2021 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1643 through Sandbox Reserved 1664. |
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