2orx: Difference between revisions
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<StructureSection load='2orx' size='340' side='right'caption='[[2orx]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2orx' size='340' side='right'caption='[[2orx]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2orx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2orx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ORX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ORX FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2orx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2orx OCA], [https://pdbe.org/2orx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2orx RCSB], [https://www.ebi.ac.uk/pdbsum/2orx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2orx ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2orx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2orx OCA], [https://pdbe.org/2orx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2orx RCSB], [https://www.ebi.ac.uk/pdbsum/2orx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2orx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/NRP1_RAT NRP1_RAT] Receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF-165 isoform of VEGF and VEGF-B. Coexpression with KDR results in increased VEGF-165 binding to KDR as well as increased chemotaxis. It may regulate VEGF-induced angiogenesis (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Bellamy HD]] | ||
[[Category: | [[Category: Jusino MA]] | ||
[[Category: Leahy | [[Category: Leahy DJ]] | ||
[[Category: Neau | [[Category: Neau DB]] | ||
[[Category: Perman | [[Category: Perman B]] | ||
[[Category: | [[Category: Vander Kooi CW]] | ||
Revision as of 13:47, 30 August 2023
Structural Basis for Ligand Binding and Heparin Mediated Activation of NeuropilinStructural Basis for Ligand Binding and Heparin Mediated Activation of Neuropilin
Structural highlights
FunctionNRP1_RAT Receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF-165 isoform of VEGF and VEGF-B. Coexpression with KDR results in increased VEGF-165 binding to KDR as well as increased chemotaxis. It may regulate VEGF-induced angiogenesis (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNeuropilin (Nrp) is a cell surface receptor with essential roles in angiogenesis and axon guidance. Interactions between Nrp and the positively charged C termini of its ligands, VEGF and semaphorin, are mediated by Nrp domains b1 and b2, which share homology to coagulation factor domains. We report here the crystal structure of the tandem b1 and b2 domains of Nrp-1 (N1b1b2) and show that they form a single structural unit. Cocrystallization of N1b1b2 with Tuftsin, a peptide mimic of the VEGF C terminus, reveals the site of interaction with the basic tail of VEGF on the b1 domain. We also show that heparin promotes N1b1b2 dimerization and map the heparin binding site on N1b1b2. These results provide a detailed picture of interactions at the core of the Nrp signaling complex and establish a molecular basis for the synergistic effects of heparin on Nrp-mediated signaling. Structural basis for ligand and heparin binding to neuropilin B domains.,Vander Kooi CW, Jusino MA, Perman B, Neau DB, Bellamy HD, Leahy DJ Proc Natl Acad Sci U S A. 2007 Apr 10;104(15):6152-7. Epub 2007 Apr 3. PMID:17405859[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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