Sandbox Reserved 1658: Difference between revisions
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<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"/>. | ||
On an other side, b1 and b2 form a jellyroll<ref name="structural study"/> <scene name='86/868191/Beta_barrel/1'>beta-barrel</scene> composes of 8 beta-sheets (<scene name='86/868191/Fin/1'>290-294 (violet), 325-330 (green), 334-342 (red), 354-363 (blue), 381-384 (orange),391-395 (cyan),399-411 (brown),418-423 (white)</scene>).One part of the domain contains three loops that typically constitute the ligand binding site for | On an other side, b1 and b2 form a jellyroll<ref name="structural study"/> <scene name='86/868191/Beta_barrel/1'>beta-barrel</scene> composes of 8 beta-sheets (<scene name='86/868191/Fin/1'>290-294 (violet), 325-330 (green), 334-342 (red), 354-363 (blue), 381-384 (orange),391-395 (cyan),399-411 (brown),418-423 (white)</scene>).One part of the domain contains three loops that typically constitute the ligand binding site for discoidin family members.</p> | ||
== Function == | == Function == | ||
<p align="justify">Neuropilins are involved in many signaling pathways. They act mainly as co-receptors because of their small cytoplasmic domain, and therefore associate with other receptors to transduce their signals through a cell membrane. Neuropilin-1 is involved in the development of the | <p align="justify">Neuropilins are involved in many signaling pathways. They act mainly as co-receptors because of their small cytoplasmic domain, and therefore associate with other receptors to transduce their signals through a cell membrane. Neuropilin-1 is involved in the development of the cardiovascular system, but also in [https://en.wikipedia.org/wiki/Angiogenesis angiogenesis] and [https://en.wikipedia.org/wiki/Organogenesis organogenesis]. It is also involved in the development of some neuronal circuits.</p> | ||
<h5>In cardiovascular development</h5> | <h5>In cardiovascular development</h5> | ||
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</p> | </p> | ||
<h5>In | <h5>In neuronal development</h5> | ||
<p align="justify">In | <p align="justify">In neuronal tissues, NRP1 associates with semaphorin-3A to perform growth cone guidance. It helps guiding axonal growth during the development of the nervous system by mediating the chemorepulsant activity of semaphorin.</p> | ||
<h5>In the immune system</h5> | <h5>In the immune system</h5> | ||
