This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox Reserved 1658
From Proteopedia
(Difference between revisions)
| Line 14: | Line 14: | ||
== 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. |
To get started:
More help: Help:Editing |
| |||||||||||
