Sandbox Reserved 1658: Difference between revisions
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Lucas Bisel (talk | contribs) No edit summary |
Lucas Bisel (talk | contribs) No edit summary |
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<Structure load='2QQI' size='350' frame='true' align='right' caption='Crystal structure of the b1/b2 domains' scene='Insert optional scene name here' /> | <Structure load='2QQI' size='350' frame='true' align='right' caption='Crystal structure of the b1/b2 domains' scene='Insert optional scene name here' /> | ||
<Structure load='2QQM' size='350' frame='true' align='right' caption='Crystal structure of a2b1b2 domains' scene='Insert optional scene name here' /> | |||
== Generalities == | == Generalities == | ||
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<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">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"> | <p align="justify"> For exemple, 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> | ||
In 2007, a study has demonstrated that the interactions between b1 and b2, and between a2 and (b1/b2) are the same for Neuropilin 1 and 2. However a1 interacts differently with the other domains and these interactions are still not really understood. | |||
The a1 and a2 domains are CUB domains and include <scene name='86/868191/Calcium_binding_site/1'>Calcium binding site</scene>. The ion is coordinated by two carbonyl oxygens from Ala(252)and Ile(253) and by three negatively charged side chains (Glu(195),Asp(209) and Asp(250)). | |||
== Function == | == Function == | ||