1wcy

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[[Image:1wcy.png|left|200px]]
 
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{{STRUCTURE_1wcy| PDB=1wcy | SCENE= }}
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==Crystal Structure Of Human Dipeptidyl Peptidase IV (DPPIV) Complex With Diprotin A==
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<StructureSection load='1wcy' size='340' side='right'caption='[[1wcy]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1wcy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WCY FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wcy OCA], [https://pdbe.org/1wcy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wcy RCSB], [https://www.ebi.ac.uk/pdbsum/1wcy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wcy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DPP4_HUMAN DPP4_HUMAN] Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.<ref>PMID:10951221</ref> <ref>PMID:17549790</ref> <ref>PMID:10570924</ref> <ref>PMID:10900005</ref> <ref>PMID:11772392</ref> <ref>PMID:14691230</ref> <ref>PMID:16651416</ref> <ref>PMID:17287217</ref> <ref>PMID:18708048</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wc/1wcy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wcy ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Dipeptidyl peptidase IV (DPPIV) is a serine protease, a member of the prolyl oligopeptidase (POP) family, and has been implicated in several diseases. Therefore, it seems important to develop selective inhibitors for human DPPIV (hDPPIV) that are able to control the biological function of hDPPIV. In order to elucidate the binding mode and substrate specificity, we determined the crystal structure complex of hDPPIV and diprotin A (IIe-Pro-IIe), a slowly hydrolyzed substrate of hDPPIV, at 2.2 A resolution. In this paper, we discuss the molecular interaction mechanism of diprotin A with hDPPIV based on the X-ray crystal structure.
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===Crystal Structure Of Human Dipeptidyl Peptidase IV (DPPIV) Complex With Diprotin A===
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The crystal structure of human dipeptidyl peptidase IV (DPPIV) complex with diprotin A.,Hiramatsu H, Yamamoto A, Kyono K, Higashiyama Y, Fukushima C, Shima H, Sugiyama S, Inaka K, Shimizu R Biol Chem. 2004 Jun;385(6):561-4. PMID:15255191<ref>PMID:15255191</ref>
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{{ABSTRACT_PUBMED_15255191}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 1wcy" style="background-color:#fffaf0;"></div>
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[[1wcy]] is a 4 chain structure of [[Dipeptidyl peptidase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCY OCA].
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==See Also==
==See Also==
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*[[Dipeptidyl peptidase|Dipeptidyl peptidase]]
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*[[Dipeptidyl peptidase 3D structures|Dipeptidyl peptidase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:015255191</ref><references group="xtra"/>
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__TOC__
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[[Category: Dipeptidyl-peptidase IV]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Fukushima, C.]]
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[[Category: Large Structures]]
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[[Category: Higashiyama, Y.]]
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[[Category: Fukushima C]]
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[[Category: Hiramatsu, H.]]
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[[Category: Higashiyama Y]]
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[[Category: Inaka, K.]]
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[[Category: Hiramatsu H]]
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[[Category: Kyono, K.]]
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[[Category: Inaka K]]
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[[Category: Shima, H.]]
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[[Category: Kyono K]]
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[[Category: Shimizu, R.]]
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[[Category: Shima H]]
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[[Category: Sugiyama, S.]]
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[[Category: Shimizu R]]
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[[Category: Yamamoto, A.]]
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[[Category: Sugiyama S]]
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[[Category: Beta-propeller structure]]
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[[Category: Yamamoto A]]
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[[Category: Cd26]]
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[[Category: Dipeptidyl peptidase iv]]
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[[Category: Diprotin some]]
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[[Category: Hydrolase]]
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[[Category: Prolyl oligopeptidase]]
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[[Category: Serine protease]]
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Current revision

Crystal Structure Of Human Dipeptidyl Peptidase IV (DPPIV) Complex With Diprotin A

PDB ID 1wcy

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