6lsq: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 6lsq is ON HOLD
+==Crystal structure of Echistatin, an RGD-containing short disintegrin==
+<StructureSection load='6lsq' size='340' side='right'caption='[[6lsq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LSQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LSQ FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6lsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lsq OCA], [https://pdbe.org/6lsq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lsq RCSB], [https://www.ebi.ac.uk/pdbsum/6lsq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lsq ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Echistatin (Ech) is a short disintegrin with a long (42)NPHKGPAT C-terminal tail. We determined the 3-D structure of Ech by X-ray crystallography. Superimposition of the structures of chains A and B showed conformational differences in their RGD loops and C-termini. The chain A structure is consistent with our NMR analysis that the GPAT residues of the C-terminus cannot be observed due to high flexibility. The hydrogen bond patterns of the RGD loop and between the RGD loop and C-terminus in Ech were the same as those of the corresponding residues in medium disintegrins. The mutant with C-terminal HKGPAT truncation caused 6.4-, 7.0-, 11.7-, and 18.6-fold decreases in inhibiting integrins alphavbeta3, alphaIIbbeta3, alphavbeta5, and alpha5beta1. Mutagenesis of the C-terminus showed that the H44A mutant caused 2.5- and 4.4-fold increases in inhibiting alphaIIbbeta3 and alpha5beta1, and the K45A mutant caused a 2.6-fold decrease in inhibiting alphaIIbbeta3. We found that Ech inhibited VEGF-induced HUVEC proliferation with an IC50 value of 103.2 nM and inhibited the migration of A375, U373MG, and Panc-1 tumor cells with IC50 values of 1.5, 5.7, and 154.5 nM. These findings suggest that Ech is a potential anticancer agent, and its C-terminal region can be optimized to improve its anticancer activity.
-Authors: Chang, Y.T., Chen, Y.C., Chuang, W.J.
+Structural Insight into Integrin Recognition and Anticancer Activity of Echistatin.,Chen YC, Chang YT, Chen CY, Shiu JH, Cheng CH, Huang CH, Chen JF, Chuang WJ Toxins (Basel). 2020 Nov 9;12(11). pii: toxins12110709. doi:, 10.3390/toxins12110709. PMID:33182321<ref>PMID:33182321</ref>
-Description: Echistatin
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Chang, Y.T]]
+<div class="pdbe-citations 6lsq" style="background-color:#fffaf0;"></div>
-[[Category: Chuang, W.J]]
-[[Category: Chen, Y.C]]
+==See Also==
+*[[Disintegrin|Disintegrin]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Chang YT]]
+[[Category: Chen YC]]
+[[Category: Chuang WJ]]