View source for 2jp5


==ATWLPPR an anti-angiogenic peptide==
<StructureSection load='2jp5' size='340' side='right'caption='[[2jp5]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2jp5]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JP5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2jp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jp5 OCA], [https://pdbe.org/2jp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jp5 RCSB], [https://www.ebi.ac.uk/pdbsum/2jp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jp5 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Heptapeptide ATWLPPR (A7R), identified in our laboratory by screening a mutated phage library, was shown to bind specifically to neuropilin-1 (NRP-1) and then to selectively inhibit VEGF(165) binding to this receptor. In vivo, treatment with A7R resulted in decreasing breast cancer angiogenesis and growth. The present work is focused on structural characterization of A7R. Analogs of the peptide, obtained by substitution of each amino acid with alanine (alanine-scanning) or by amino acid deletion, have been systematically assayed to determine the relative importance of the side chains of each residue with respect to the inhibitory effect of A7R on VEGF(165) binding to NRP-1. We show here the importance of the C-terminal sequence LPPR and particularly the key role of C-terminal arginine. In solution, A7R displays significant secondary structure of the backbone adopting an extended conformation. However, the functional groups of arginine are very flexible in the absence of NRP-1 pointing to an induced fit upon binding to the receptor. A MD trajectory of the A7R/NRP-1 complex in explicit water, based on the recent tuftsin/NRP-1 crystal structure, has revealed the hydrogen-bonding network that contributes to A7R's binding activity.

Structure-function analysis of the antiangiogenic ATWLPPR peptide inhibiting VEGF(165) binding to neuropilin-1 and molecular dynamics simulations of the ATWLPPR/neuropilin-1 complex.,Starzec A, Ladam P, Vassy R, Badache S, Bouchemal N, Navaza A, du Penhoat CH, Perret GY Peptides. 2007 Dec;28(12):2397-402. Epub 2007 Sep 29. PMID:17983687<ref>PMID:17983687</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2jp5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Badache S]]
[[Category: Bouchemal NC]]
[[Category: Herve du Penhoat CLM]]