2f1g: Difference between revisions
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<StructureSection load='2f1g' size='340' side='right'caption='[[2f1g]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2f1g' size='340' side='right'caption='[[2f1g]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2f1g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2f1g]] 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=2F1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F1G FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNF:N~2~-1,3-BENZOXAZOL-2-YL-3-CYCLOHEXYL-N-{2-[(4-METHOXYPHENYL)AMINO]ETHYL}-L-ALANINAMIDE'>GNF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNF:N~2~-1,3-BENZOXAZOL-2-YL-3-CYCLOHEXYL-N-{2-[(4-METHOXYPHENYL)AMINO]ETHYL}-L-ALANINAMIDE'>GNF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2f1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1g OCA], [https://pdbe.org/2f1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f1g RCSB], [https://www.ebi.ac.uk/pdbsum/2f1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f1g 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=2f1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1g OCA], [https://pdbe.org/2f1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f1g RCSB], [https://www.ebi.ac.uk/pdbsum/2f1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f1g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f1/2f1g_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f1/2f1g_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Clark | [[Category: Clark K]] | ||
[[Category: Harris | [[Category: Harris JL]] | ||
[[Category: Hornsby | [[Category: Hornsby M]] | ||
[[Category: Karenewsky | [[Category: Karenewsky DS]] | ||
[[Category: Kulathila | [[Category: Kulathila R]] | ||
[[Category: Lesley | [[Category: Lesley SA]] | ||
[[Category: Spraggon | [[Category: Spraggon G]] | ||
[[Category: Tully | [[Category: Tully DC]] | ||
Latest revision as of 10:36, 9 October 2024
Cathepsin S in complex with non-covalent 2-(Benzoxazol-2-ylamino)-acetamideCathepsin S in complex with non-covalent 2-(Benzoxazol-2-ylamino)-acetamide
Structural highlights
FunctionCATS_HUMAN Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N. 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 PubMedA series of N(alpha)-2-benzoxazolyl-alpha-amino acid-(arylaminoethyl)amides were identified as potent, selective, and noncovalent inhibitors of cathepsin S. Structure-activity relationships including strategies for modulating the selectivities among cathepsins S, K, and L, and in vivo pharmacokinetics are discussed. A X-ray structure of compound 3 bound to the active site of cathepsin S is also reported. Synthesis and evaluation of arylaminoethyl amides as noncovalent inhibitors of cathepsin S. Part 3: heterocyclic P3.,Tully DC, Liu H, Alper PB, Chatterjee AK, Epple R, Roberts MJ, Williams JA, Nguyen KT, Woodmansee DH, Tumanut C, Li J, Spraggon G, Chang J, Tuntland T, Harris JL, Karanewsky DS Bioorg Med Chem Lett. 2006 Apr 1;16(7):1975-80. Epub 2006 Jan 30. PMID:16446091[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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