1sp4
From Proteopedia
(Difference between revisions)
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<StructureSection load='1sp4' size='340' side='right'caption='[[1sp4]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1sp4' size='340' side='right'caption='[[1sp4]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1sp4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1sp4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SP4 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EP2:METHYL+N-[(2S)-4-{[(1S)-1-{[(2S)-2-CARBOXYPYRROLIDIN-1-YL]CARBONYL}-3-METHYLBUTYL]AMINO}-2-HYDROXY-4-OXOBUTANOYL]-L-LEUCYLGLYCYLGLYCINATE'>EP2</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]] 2.2Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EP2:METHYL+N-[(2S)-4-{[(1S)-1-{[(2S)-2-CARBOXYPYRROLIDIN-1-YL]CARBONYL}-3-METHYLBUTYL]AMINO}-2-HYDROXY-4-OXOBUTANOYL]-L-LEUCYLGLYCYLGLYCINATE'>EP2</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=1sp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sp4 OCA], [https://pdbe.org/1sp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sp4 RCSB], [https://www.ebi.ac.uk/pdbsum/1sp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sp4 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=1sp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sp4 OCA], [https://pdbe.org/1sp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sp4 RCSB], [https://www.ebi.ac.uk/pdbsum/1sp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sp4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/CATB_BOVIN CATB_BOVIN] Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1sp4 ConSurf]. | </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=1sp4 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The crystal structure of the inhibitor NS-134 in complex with bovine cathepsin B reveals that functional groups attached to both sides of the epoxysuccinyl reactive group bind to the part of active-site cleft as predicted. The -Leu-Pro-OH side binds to the primed binding sites interacting with the His110 and His111 residues with its C-terminal carboxy group, whereas the -Leu-Gly-Meu (-Leu-Gly-Gly-OMe) part (Meu, methoxycarbonylmethyl) binds along the non-primed binding sites. Comparison with the propeptide structures of cathepsins revealed that the binding of the latter part is least similar to the procathepsin B structure; this result, together with the two-residue shift in positioning of the Leu-Gly-Gly part, suggests that the propeptide structures of the cognate enzymes may not be the best starting point for the design of reverse binding inhibitors. | ||
- | |||
- | Crystal structure of NS-134 in complex with bovine cathepsin B: a two-headed epoxysuccinyl inhibitor extends along the entire active-site cleft.,Stern I, Schaschke N, Moroder L, Turk D Biochem J. 2004 Jul 15;381(Pt 2):511-7. PMID:15084146<ref>PMID:15084146</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1sp4" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Cathepsin 3D structures|Cathepsin 3D structures]] | *[[Cathepsin 3D structures|Cathepsin 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Bos taurus]] |
- | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Moroder | + | [[Category: Moroder L]] |
- | [[Category: Schaschke | + | [[Category: Schaschke N]] |
- | [[Category: Stern | + | [[Category: Stern I]] |
- | [[Category: Turk | + | [[Category: Turk D]] |
- | + | ||
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Revision as of 13:29, 13 March 2024
Crystal structure of NS-134 in complex with bovine cathepsin B: a two headed epoxysuccinyl inhibitor extends along the whole active site cleft
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