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1okx
From Proteopedia
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| - | [[ | + | ==BINDING STRUCTURE OF ELASTASE INHIBITOR SCYPTOLIN A== |
| + | <StructureSection load='1okx' size='340' side='right' caption='[[1okx]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1okx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Scytonema_hofmanni Scytonema hofmanni] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OKX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OKX FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=1BO:1-BUTANOL'>1BO</scene>, <scene name='pdbligand=CNT:N-METHYL-META-CHLORO-TYROSINE'>CNT</scene>, <scene name='pdbligand=SUJ:(2R,3R)-2-[(3S,6R)-3-AMINO-6-HYDROXY-2-OXOPIPERIDINYL]-3-HYDROXYBUTANOIC+ACID'>SUJ</scene></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b0e|1b0e]], [[1bma|1bma]], [[1btu|1btu]], [[1c1m|1c1m]], [[1e34|1e34]], [[1e35|1e35]], [[1e36|1e36]], [[1e37|1e37]], [[1e38|1e38]], [[1eai|1eai]], [[1eas|1eas]], [[1eat|1eat]], [[1eau|1eau]], [[1ela|1ela]], [[1elb|1elb]], [[1elc|1elc]], [[1eld|1eld]], [[1ele|1ele]], [[1elf|1elf]], [[1elg|1elg]], [[1esa|1esa]], [[1esb|1esb]], [[1est|1est]], [[1fle|1fle]], [[1fzz|1fzz]], [[1gvk|1gvk]], [[1gwa|1gwa]], [[1h9l|1h9l]], [[1hax|1hax]], [[1hay|1hay]], [[1haz|1haz]], [[1hb0|1hb0]], [[1hv7|1hv7]], [[1inc|1inc]], [[1jim|1jim]], [[1l0z|1l0z]], [[1l1g|1l1g]], [[1lka|1lka]], [[1lkb|1lkb]], [[1lvy|1lvy]], [[1mcv|1mcv]], [[1mmj|1mmj]], [[1nes|1nes]], [[1qgf|1qgf]], [[1qix|1qix]], [[1qnj|1qnj]], [[1qr3|1qr3]], [[2est|2est]], [[3est|3est]], [[4est|4est]], [[5est|5est]], [[6est|6est]], [[7est|7est]], [[8est|8est]], [[9est|9est]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1okx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1okx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1okx RCSB], [http://www.ebi.ac.uk/pdbsum/1okx PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ok/1okx_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Natural bioactive compounds are of general interest to pharmaceutical research because they may be used as leads in drug development campaigns. Among them, scyptolin A and B from Scytonema hofmanni PCC 7110 are known to inhibit porcine pancreatic elastase, which in turn resembles the attractive drug target neutrophil elastase. The crystal structure of scyptolin A as bound to pancreatic elastase was solved at 2.8 A resolution. The inhibitor occupies the most prominent subsites S1 through S4 of the elastase and prevents a hydrolytic attack by covering the active center with its rigid ring structure. The observed binding structure may help to design potent elastase inhibitors. | ||
| - | + | Binding structure of elastase inhibitor scyptolin A.,Matern U, Schleberger C, Jelakovic S, Weckesser J, Schulz GE Chem Biol. 2003 Oct;10(10):997-1001. PMID:14583266<ref>PMID:14583266</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Elastase|Elastase]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
| - | < | + | |
[[Category: Pancreatic elastase]] | [[Category: Pancreatic elastase]] | ||
[[Category: Scytonema hofmanni]] | [[Category: Scytonema hofmanni]] | ||
Revision as of 15:18, 28 September 2014
BINDING STRUCTURE OF ELASTASE INHIBITOR SCYPTOLIN A
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