Sandbox Reserved 1658: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Tina Le Gall (talk | contribs) No edit summary |
Tina Le Gall (talk | contribs) No edit summary |
||
| Line 18: | Line 18: | ||
<p align="justify">Neuropilin-1 has three different domains<ref name="structural study"/>. A cytoplasmic domain which contains 40 residues, a transmembrane domain which contains 24 residues and a 850-residues ectodomain<ref name="human neuropilin">Christian C. Lee, Andreas Kreusch,Daniel McMullan, Ken Ng, and Glen Spraggon Crystal Structure of the HumanNeuropilin-1 b1 Domain https://www.cell.com/structure/pdf/S0969-2126(02)00941-3.pdf</ref>. The latter is an assembly of five individual motifs (a1,<scene name='86/868191/Domaine_a2/1'>a2</scene>,<scene name='86/868191/Domaine_b1/1'>b1</scene>,<scene name='86/868191/Domaine_b2/1'>b2</scene> and c). It contains, hence two [https://en.wikipedia.org/wiki/CUB_domain CUB domains] (a1/a2), two homologous domains to coagulation factors V/VIII (b1/b2) and a [https://en.wikipedia.org/wiki/MAM_domain MAM domain] (c). The ligand binding is mediated by the (a1/a2) and (b1/b2) portion of the ectodomain while the c domain mediates Neuropilin [https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/oligomerization oligomerization]. However MAM domain isn't able to support on its own multimerization of NRP molecules. So, it might contribute to the assembly and regulation of the signaling complexes by positionning the other extracellular domains of NRPs away from the membrane.<ref name="MAM domain">PMID: 27720589</ref></p> | <p align="justify">Neuropilin-1 has three different domains<ref name="structural study"/>. A cytoplasmic domain which contains 40 residues, a transmembrane domain which contains 24 residues and a 850-residues ectodomain<ref name="human neuropilin">Christian C. Lee, Andreas Kreusch,Daniel McMullan, Ken Ng, and Glen Spraggon Crystal Structure of the HumanNeuropilin-1 b1 Domain https://www.cell.com/structure/pdf/S0969-2126(02)00941-3.pdf</ref>. The latter is an assembly of five individual motifs (a1,<scene name='86/868191/Domaine_a2/1'>a2</scene>,<scene name='86/868191/Domaine_b1/1'>b1</scene>,<scene name='86/868191/Domaine_b2/1'>b2</scene> and c). It contains, hence two [https://en.wikipedia.org/wiki/CUB_domain CUB domains] (a1/a2), two homologous domains to coagulation factors V/VIII (b1/b2) and a [https://en.wikipedia.org/wiki/MAM_domain MAM domain] (c). The ligand binding is mediated by the (a1/a2) and (b1/b2) portion of the ectodomain while the c domain mediates Neuropilin [https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/oligomerization oligomerization]. However MAM domain isn't able to support on its own multimerization of NRP molecules. So, it might contribute to the assembly and regulation of the signaling complexes by positionning the other extracellular domains of NRPs away from the membrane.<ref name="MAM domain">PMID: 27720589</ref></p> | ||
<p align="justify"> For example, the semaphorins (SEMA) bind to the (a1/a2/b1) domains while Vascular endothelial growth factors (VEGFs) bind to (b1/b2)<ref name="structural study"/>. The c domain as well as the transmembrane domain, is involved in the receptor dimerization. The cytoplasmic domain does not contain a binding domain but a [https://en.wikipedia.org/wiki/PDZ_domain PDZ domain]. This segment is only 42-44 amino acids length and by the way hasn't any catalytic function. It participates in the formation and stimulation of signalling complexes.</p> | <p align="justify"> For example, the [https://en.wikipedia.org/wiki/Semaphorin semaphorins] (SEMA) bind to the (a1/a2/b1) domains while Vascular endothelial growth factors (VEGFs) bind to (b1/b2)<ref name="structural study"/>. The c domain as well as the transmembrane domain, is involved in the receptor dimerization. The cytoplasmic domain does not contain a binding domain but a [https://en.wikipedia.org/wiki/PDZ_domain PDZ domain]. This segment is only 42-44 amino acids length and by the way hasn't any catalytic function. It participates in the formation and stimulation of signalling complexes.</p> | ||
<p align="justify">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. | <p align="justify">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><ref name="structural study"/>. 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))<ref name="structural study"/>. | The a1 and a2 domains are CUB domains and include <scene name='86/868191/Calcium_binding_site/1'>Calcium binding site</scene><ref name="structural study"/>. 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))<ref name="structural study"/>. | ||
