4qds: Difference between revisions

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'''Unreleased structure'''
==Physical basis for Nrp2 ligand binding==
<StructureSection load='4qds' size='340' side='right' caption='[[4qds]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qds]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QDS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QDS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qdr|4qdr]], [[4qdq|4qdq]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qds OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qds RCSB], [http://www.ebi.ac.uk/pdbsum/4qds PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/NRP2_HUMAN NRP2_HUMAN]] High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Vascular endothelial growth factor C (VEGF-C) is a potent lymphangiogenic cytokine that signals via the coordinated action of two cell surface receptors, Neuropilin-2 (Nrp2) and VEGFR-3. Diseases associated with both loss and gain of VEGF-C function, lymphedema and cancer, respectively, motivate studies of VEGF-C/Nrp2 binding and inhibition. Here, we demonstrate that VEGF-C binding to Nrp2 is regulated by C-terminal proteolytic maturation. The structure of the VEGF-C C terminus in complex with the ligand binding domains of Nrp2 demonstrates that a cryptic Nrp2 binding motif is released upon proteolysis, allowing specific engagement with the b1 domain of Nrp2. Based on the identified structural requirements for Nrp2 binding to VEGF-C, we hypothesized that the endogenous secreted splice form of Nrp2, s9Nrp2, may function as a selective inhibitor of VEGF-C. We find that s9Nrp2 forms a stable dimer that potently inhibits VEGF-C/Nrp2 binding and cellular signaling. These data provide critical insight into VEGF-C/Nrp2 binding and inhibition.


The entry 4qds is ON HOLD  until Paper Publication
Structural Basis for VEGF-C Binding to Neuropilin-2 and Sequestration by a Soluble Splice Form.,Parker MW, Linkugel AD, Goel HL, Wu T, Mercurio AM, Vander Kooi CW Structure. 2015 Apr 7;23(4):677-87. doi: 10.1016/j.str.2015.01.018. Epub 2015 Mar, 5. PMID:25752543<ref>PMID:25752543</ref>


Authors: Parker, M.W., Vander Kooi, C.W.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Physical basis for Nrp2 ligand binding
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Parker, M.W]]
__TOC__
[[Category: Vander Kooi, C.W]]
</StructureSection>
[[Category: Kooi, C W.Vander]]
[[Category: Parker, M W]]
[[Category: Cell adhesion]]
[[Category: Coagulation factor domain]]
[[Category: Discoidin domain]]
[[Category: Receptor]]
[[Category: Secreted]]
[[Category: Vegf-c]]
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