1pfq

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[[Image:1pfq.gif|left|200px]]
 
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==crystal structure of human apo dipeptidyl peptidase IV / CD26==
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The line below this paragraph, containing "STRUCTURE_1pfq", creates the "Structure Box" on the page.
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<StructureSection load='1pfq' size='340' side='right'caption='[[1pfq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1pfq]] is a 2 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=1PFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PFQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.9&#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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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{{STRUCTURE_1pfq| PDB=1pfq | SCENE= }}
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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=1pfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pfq OCA], [https://pdbe.org/1pfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pfq RCSB], [https://www.ebi.ac.uk/pdbsum/1pfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pfq 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/pf/1pfq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1pfq ConSurf].
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<div style="clear:both"></div>
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'''crystal structure of human apo dipeptidyl peptidase IV / CD26'''
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==See Also==
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*[[Dipeptidyl peptidase 3D structures|Dipeptidyl peptidase 3D structures]]
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== References ==
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==Overview==
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<references/>
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Dipeptidyl peptidase IV is a multifunctional type II transmembrane serine protease glycoprotein. The high-resolution crystal structure of the homodimeric human apo dipeptidyl peptidase IV has been determined at 1.9 A resolution. In addition, the structure of the binary complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-cyano-(S)-pyrrol idine has been solved, revealing the nature of the covalent interaction with the active-site serine.
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__TOC__
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</StructureSection>
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==About this Structure==
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1PFQ is a [[Single protein]] structure of 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=1PFQ OCA].
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==Reference==
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High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-cyano-(S)-pyrrol idine., Oefner C, D'Arcy A, Mac Sweeney A, Pierau S, Gardiner R, Dale GE, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1206-12. Epub 2003, Jun 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12832764 12832764]
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[[Category: Dipeptidyl-peptidase IV]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Arcy, A D.]]
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[[Category: D'Arcy A]]
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[[Category: Dale, G E.]]
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[[Category: Dale GE]]
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[[Category: Gardiner, R.]]
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[[Category: Gardiner R]]
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[[Category: Oefner, C.]]
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[[Category: Mac Sweeney A]]
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[[Category: Pierau, S.]]
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[[Category: Oefner C]]
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[[Category: Sweeney, A Mac.]]
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[[Category: Pierau S]]
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[[Category: Mch_1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:02:02 2008''
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Current revision

crystal structure of human apo dipeptidyl peptidase IV / CD26

PDB ID 1pfq

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