2buc
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2buc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUC FirstGlance]. <br> | <table><tr><td colspan='2'>[[2buc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUC FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=008:(S)-2-[(R)-3-AMINO-4-(2-FLUORO-PHENYL)-BUTYRYL]-1,2,3,4-TETRAHYDRO-ISOQUINOLINE-3-CARBOXYLIC+ACID+AMIDE'>008</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=008:(S)-2-[(R)-3-AMINO-4-(2-FLUORO-PHENYL)-BUTYRYL]-1,2,3,4-TETRAHYDRO-ISOQUINOLINE-3-CARBOXYLIC+ACID+AMIDE'>008</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2buc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2buc OCA], [https://pdbe.org/2buc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2buc RCSB], [https://www.ebi.ac.uk/pdbsum/2buc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2buc ProSAT]</span></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=2buc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2buc OCA], [https://pdbe.org/2buc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2buc RCSB], [https://www.ebi.ac.uk/pdbsum/2buc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2buc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/DPP4_PIG DPP4_PIG] 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 (By similarity). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.<ref>PMID:14719797</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Dipeptidyl-peptidase IV]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
| - | [[Category: Cerezo-Galvez | + | [[Category: Cerezo-Galvez S]] |
| - | [[Category: Edwards | + | [[Category: Edwards PJ]] |
| - | [[Category: Feurer | + | [[Category: Feurer A]] |
| - | [[Category: Hill | + | [[Category: Hill O]] |
| - | [[Category: Matassa | + | [[Category: Matassa VG]] |
| - | [[Category: Metz | + | [[Category: Metz G]] |
| - | [[Category: Nordhoff | + | [[Category: Nordhoff S]] |
| - | [[Category: Rummey | + | [[Category: Rummey C]] |
| - | [[Category: Thiemann | + | [[Category: Thiemann M]] |
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Revision as of 11:23, 22 May 2024
Crystal Structure Of Porcine Dipeptidyl Peptidase IV (CD26) in Complex with a Tetrahydroisoquinoline Inhibitor
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Categories: Large Structures | Sus scrofa | Cerezo-Galvez S | Edwards PJ | Feurer A | Hill O | Matassa VG | Metz G | Nordhoff S | Rummey C | Thiemann M
