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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[1wpx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WPX FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1wpx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WPX FirstGlance]. <br> |
| - | </td></tr><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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bd9|1bd9]], [[1beh|1beh]], [[1a44|1a44]], [[1qou|1qou]], [[1fjj|1fjj]], [[1fux|1fux]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Carboxypeptidase_C Carboxypeptidase C], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.5 3.4.16.5] </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=1wpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wpx OCA], [https://pdbe.org/1wpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wpx RCSB], [https://www.ebi.ac.uk/pdbsum/1wpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wpx 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=1wpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wpx OCA], [https://pdbe.org/1wpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wpx RCSB], [https://www.ebi.ac.uk/pdbsum/1wpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wpx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CBPY_YEAST CBPY_YEAST]] Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate. [[https://www.uniprot.org/uniprot/CPYI_YEAST CPYI_YEAST]] Specific and potent inhibitor of carboxypeptidase Y.<ref>PMID:9521655</ref>
| + | [https://www.uniprot.org/uniprot/CBPY_YEAST CBPY_YEAST] Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate. |
| | == 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: Carboxypeptidase C]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Fujii, T]] | + | [[Category: Fujii T]] |
| - | [[Category: Hata, Y]] | + | [[Category: Hata Y]] |
| - | [[Category: Hayashi, R]] | + | [[Category: Hayashi R]] |
| - | [[Category: Hayashida, M]] | + | [[Category: Hayashida M]] |
| - | [[Category: Mima, J]] | + | [[Category: Mima J]] |
| - | [[Category: Narita, Y]] | + | [[Category: Narita Y]] |
| - | [[Category: Ueda, M]] | + | [[Category: Ueda M]] |
| - | [[Category: Carboxypeptidase inhibitor]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Phosphatidylethanolamine-binding protein]]
| + | |
| - | [[Category: Phospholipid]]
| + | |
| - | [[Category: Proteinase-inhibitor complex]]
| + | |
| - | [[Category: Serine proteinase inhibitor]]
| + | |
| Structural highlights
Function
CBPY_YEAST Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Carboxypeptidase Y (CPY) inhibitor, IC, shows no homology to any other known proteinase inhibitors and rather belongs to the phosphatidylethanolamine-binding protein (PEBP) family. We report here on the crystal structure of the IC-CPY complex at 2.7 A resolution. The structure of IC in the complex with CPY consists of one major beta-type domain and a N-terminal helical segment. The structure of the complex contains two binding sites of IC toward CPY, the N-terminal inhibitory reactive site (the primary CPY-binding site) and the secondary CPY-binding site, which interact with the S1 substrate-binding site of CPY and the hydrophobic surface flanked by the active site of the enzyme, respectively. It was also revealed that IC had the ligand-binding site, which is conserved among PEBPs and the putative binding site of the polar head group of phospholipid. The complex structure and analyses of IC mutants for inhibitory activity and the binding to CPY demonstrate that the N-terminal inhibitory reactive site is essential both for inhibitory function and the complex formation with CPY and that the binding of IC to CPY constitutes a novel mode of the proteinase-protein inhibitor interaction. The unique binding mode of IC toward the cognate proteinase provides insights into the inhibitory mechanism of PEBPs toward serine proteinases and into the specific biological functions of IC belonging to the PEBP family as well.
Structure of the carboxypeptidase Y inhibitor IC in complex with the cognate proteinase reveals a novel mode of the proteinase-protein inhibitor interaction.,Mima J, Hayashida M, Fujii T, Narita Y, Hayashi R, Ueda M, Hata Y J Mol Biol. 2005 Mar 11;346(5):1323-34. Epub 2005 Jan 25. PMID:15713484[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mima J, Hayashida M, Fujii T, Narita Y, Hayashi R, Ueda M, Hata Y. Structure of the carboxypeptidase Y inhibitor IC in complex with the cognate proteinase reveals a novel mode of the proteinase-protein inhibitor interaction. J Mol Biol. 2005 Mar 11;346(5):1323-34. Epub 2005 Jan 25. PMID:15713484 doi:10.1016/j.jmb.2004.12.051
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