Neuropilin
From Proteopedia
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== Relevance == | == Relevance == | ||
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 == | ||
| + | NPR structure contains the extracellular domains A1, A2 which bind semaphorin; B1, B2 which bind VEGF and C which is the dimerization region. | ||
== 3D Structures of Neuropilin == | == 3D Structures of Neuropilin == | ||
Revision as of 10:36, 10 May 2016
Contents |
Function
Neuropilin (NRP) are neuronal receptors. NRP are co-receptors for semaphorins[1]. There are 2 classes of NRP – NRP-1 and NRP-2.
- NRP-1 has high affinity for semaphorin-3A.
- NRP-2 has high affinity for semaphorin-3F.
Relevance
NRP are highly expressed in human neoplasms[2].
Structural highlights
NPR structure contains the extracellular domains A1, A2 which bind semaphorin; B1, B2 which bind VEGF and C which is the dimerization region.
3D Structures of Neuropilin
Updated on 10-May-2016
References
- ↑ Romeo PH, Lemarchandel V, Tordjman R. Neuropilin-1 in the immune system. Adv Exp Med Biol. 2002;515:49-54. PMID:12613542
- ↑ 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
