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New page: left|200px<br /><applet load="1bma" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bma, resolution 1.8Å" /> '''BENZYL METHYL AMINIMI... |
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== | ==BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASE== | ||
The crystal structure of an aminimide analog of a dipeptide inhibitor of | <StructureSection load='1bma' size='340' side='right'caption='[[1bma]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1bma]] is a 1 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=1BMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BMA FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QH:(1R)-1-BENZYL-1-METHYL-1-(2-{[4-(1-METHYLETHYL)PHENYL]AMINO}-2-OXOETHYL)-2-{(2S)-4-METHYL-2-[(TRIFLUOROACETYL)AMINO]PENTANOYL}DIAZANIUM'>0QH</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1bma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bma OCA], [https://pdbe.org/1bma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bma RCSB], [https://www.ebi.ac.uk/pdbsum/1bma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bma ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG] Acts upon elastin. | |||
== 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/bm/1bma_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=1bma ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of an aminimide analog of a dipeptide inhibitor of porcine pancreatic elastase bound to its target serine protease has been solved. The peptidomimetic molecule binds in the same fashion as the class of dipeptides from which it was derived, making similar interactions with the subsites on the elastase surface. Because aminimides are readily synthesized from a wide variety of starting materials, they form the basis for a combinatorial chemistry approach to rational drug design. | |||
Interaction of a peptidomimetic aminimide inhibitor with elastase.,Peisach E, Casebier D, Gallion SL, Furth P, Petsko GA, Hogan JC Jr, Ringe D Science. 1995 Jul 7;269(5220):66-9. PMID:7604279<ref>PMID:7604279</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[ | <div class="pdbe-citations 1bma" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
==See Also== | |||
*[[Elastase 3D structures|Elastase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Casebier | [[Category: Casebier D]] | ||
[[Category: Furth | [[Category: Furth P]] | ||
[[Category: Gallion | [[Category: Gallion SL]] | ||
[[Category: | [[Category: Hogan Jr JC]] | ||
[[Category: Peisach | [[Category: Peisach E]] | ||
[[Category: Petsko | [[Category: Petsko GA]] | ||
[[Category: Ringe | [[Category: Ringe D]] | ||
Latest revision as of 10:18, 23 October 2024
BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASEBENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASE
Structural highlights
FunctionCELA1_PIG Acts upon elastin. 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 PubMedThe crystal structure of an aminimide analog of a dipeptide inhibitor of porcine pancreatic elastase bound to its target serine protease has been solved. The peptidomimetic molecule binds in the same fashion as the class of dipeptides from which it was derived, making similar interactions with the subsites on the elastase surface. Because aminimides are readily synthesized from a wide variety of starting materials, they form the basis for a combinatorial chemistry approach to rational drug design. Interaction of a peptidomimetic aminimide inhibitor with elastase.,Peisach E, Casebier D, Gallion SL, Furth P, Petsko GA, Hogan JC Jr, Ringe D Science. 1995 Jul 7;269(5220):66-9. PMID:7604279[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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