Neuropilin

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{{STRUCTURE_2qqm| PDB=2qqm | SIZE=400| SCENE= |right|CAPTION=Human glycosylated neuropilin-1 domains A2,B1,B2 complex with ethylene glycol and Ca+2 ion (green) [[2qqm]] }}
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<StructureSection load='' size='350' side='right' scene='46/466529/Cv/1' caption='Human glycosylated neuropilin-1 domains A2,B1,B2 complex with ethylene glycol and Ca+2 ion (green) [[2qqm]]'>
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== Function ==
== Function ==
'''Neuropilin''' (NRP) are neuronal receptors. NRP are co-receptors for semaphorins<ref>PMID:12613542</ref>. There are 2 classes of NRP – NRP-1 and NRP-2.<br />
'''Neuropilin''' (NRP) are neuronal receptors. NRP are co-receptors for semaphorins<ref>PMID:12613542</ref>. There are 2 classes of NRP – NRP-1 and NRP-2.<br />
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NRP are highly expressed in human neoplasms<ref>PMID:18363553</ref>.
NRP are highly expressed in human neoplasms<ref>PMID:18363553</ref>.
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== Structural highlights ==
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NPR structure contains the extracellular domains A1, A2 which bind semaphorin; B1, B2 which bind VEGF and C which is the dimerization region.
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*<scene name='46/466529/Cv/3'>Ca coordination site</scene>. Water molecule are shown as red sphere.
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</StructureSection>
== 3D Structures of Neuropilin ==
== 3D Structures of Neuropilin ==
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{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|
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*NRP-1
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*NRP-1; Domains - B1 273-427, MAM 628-813, A2B1B2 141-586
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**[[1kex]], [[2qqi]] – hNRP-1 B domain – human
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**[[2qqm]] - hNRP-1 A+B domain<br />
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**[[4deq]] - hNRP-1 B domain + VEGF-A heparin-binding domain<br />
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**[[2qqn]] - hNRP-1 B domain + VEGF-blocking antibody
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**[[3i97]] - hNRP-1 B domains + inhibitor
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**[[1kex]], [[2qqi]] – hNRP-1 B1 domain – human<br />
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**[[4rn5]] – hNRP-1 B1 domain<br />
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**[[7o1n]] – hNRP-1 B1 domain (mutant)<br />
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**[[5l73]] – hNRP-1 MAM domain<br />
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**[[2qqm]] - hNRP-1 A2+B1+B2 domains<br />
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**[[4deq]] - hNRP-1 B1 domain + VEGF-A heparin-binding domain<br />
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**[[6tkk]] - hNRP-1 B1 domain + VEGF-A peptide<br />
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**[[7p5u]] - hNRP-1 B1 domain + VEGF-B peptide<br />
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**[[7jjc]] - hNRP-1 B1 domain + SARS-CoV-2 peptide<br />
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**[[2qqn]] - hNRP-1 B1 domain + VEGF-blocking antibody
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**[[5c7g]] – hNRP-1 B1 domain + bicine<br />
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**[[5ijr]], [[5iyy]], [[5j1x]], [[5jgi]], [[5jgq]], [[5jhk]] – hNRP-1 B1 domain + arginine derivative<br />
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**[[3i97]], [[6fmc]], [[6fmf]] - hNRP-1 B1 domains + inhibitor
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**[[2orx]] – rNRP-1 C1+C2 domains – rat
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**[[2orx]] – rNRP-1 B domains – rat
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**[[2orz]] – rNRP-1 + tuftsin peptide<br />
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**[[2orz]] – rNRP-1 B domains + tuftsin peptide<br />
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**[[4gz9]] - mNRP-1 A+B domain – mouse<br />
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**[[4gz9]] - mNRP-1 – mouse<br />
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**[[4gza]] - mNRP-1 A+B domain + plexin A2 + semaphorin 3A
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**[[4gza]] - mNRP-1 + plexin A2 + semaphorin 3A<br />
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**[[7m0r]] – mNRP-1 + Semaphorin 3A + plexin A4 – Cryo EM<br />
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*NRP-2
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*NRP-2; Domains - CUB 27-145; A2 145-275; B1 275-430; B2 431-595
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**[[2qqj]], [[4qdq]], [[4qds]] - hNRP-2 B domain<br />
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**[[7t4s]] – hNRP-2 + Herpes virus envelope + antibody – Cryo EM<br />
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**[[4qdr]] - hNRP-2 B domain (mutant)<br />
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**[[4qdq]], [[4qds]], [[2qqj]] - hNRP-2 B1+B2 domains<br />
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**[[2qqo]] - hNRP-2 A+B domains
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**[[5dq0]] – hNRP-2 B1 domain<br />
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**[[4qdr]] - hNRP-2 B1+B2 domain (mutant)<br />
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**[[2qqo]] - hNRP-2 A2+B1+B2 domains
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**[[2qqk]], [[2qql]] - hNRP-2 A+B domains + semaphorin-blocking antibody
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**[[2qqk]], [[2qql]] - hNRP-2 A2+B1+B2 domains + semaphorin-blocking antibody<br />
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**[[5dn2]], [[6tdb]], [[6tjt]] – hNRP-2 B1 domain + VEGF-A C terminal<br />
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**[[6gh8]] – hNRP-2 CUB domain 1 + Gp1<br />
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**[[7m22]] – mNRP-2 + cytomegalovirus – Cryo EM<br />
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human glycosylated neuropilin-1 domains A2,B1,B2 complex with ethylene glycol and Ca+2 ion (green) 2qqm

Drag the structure with the mouse to rotate

3D Structures of Neuropilin

Updated on 16-July-2023

References

  1. ↑ Romeo PH, Lemarchandel V, Tordjman R. Neuropilin-1 in the immune system. Adv Exp Med Biol. 2002;515:49-54. PMID:12613542
  2. ↑ Pellet-Many C, Frankel P, Jia H, Zachary I. Neuropilins: structure, function and role in disease. Biochem J. 2008 Apr 15;411(2):211-26. doi: 10.1042/BJ20071639. PMID:18363553 doi:http://dx.doi.org/10.1042/BJ20071639

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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