4aig: Difference between revisions
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==ADAMALYSIN II WITH PHOSPHONATE INHIBITOR== | |||
[[Image: | <StructureSection load='4aig' size='340' side='right' caption='[[4aig]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4aig]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Crotalus_adamanteus Crotalus adamanteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AIG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AIG FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FLX:N-[(FURAN-2-YL)CARBONYL]-(S)-LEUCYL-(R)-[1-AMINO-2(1H-INDOL-3-YL)ETHYL]-PHOSPHONIC+ACID'>FLX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adamalysin Adamalysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.46 3.4.24.46] </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=4aig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aig OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4aig RCSB], [http://www.ebi.ac.uk/pdbsum/4aig 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/ai/4aig_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 == | |||
The search of reprolysin inhibitors offers the possibility of intervention against both matrixins and ADAMs. Here we report the crystal structure of the complex between adamalysin II, a member of the reprolysin family, and a phosphonate inhibitor modeled on an endogenous venom tripeptide. The inhibitor occupies the primed region of the cleavage site adopting a retro-binding mode. The phosphonate group ligates the zinc ion in an asymmetric bidentate mode and the adjacent Trp indole system partly fills the primary specificity subsite S1'. An adamalysin-based model of tumor necrosis factor-alpha-converting enzyme (TACE) reveals a smaller S1' pocket for this enzyme. | |||
2 angstrom X-ray structure of adamalysin II complexed with a peptide phosphonate inhibitor adopting a retro-binding mode.,Cirilli M, Gallina C, Gavuzzo E, Giordano C, Gomis-Ruth FX, Gorini B, Kress LF, Mazza F, Paradisi MP, Pochetti G, Politi V FEBS Lett. 1997 Dec 1;418(3):319-22. PMID:9428736<ref>PMID:9428736</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Adamalysin]] | [[Category: Adamalysin]] | ||
[[Category: Crotalus adamanteus]] | [[Category: Crotalus adamanteus]] | ||
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[[Category: Mazza, F.]] | [[Category: Mazza, F.]] | ||
[[Category: Pochetti, G.]] | [[Category: Pochetti, G.]] | ||
[[Category: Metalloendopeptidase]] | |||
[[Category: Snake venom metalloendopeptidase]] | [[Category: Snake venom metalloendopeptidase]] | ||
[[Category: Zinc protease]] | [[Category: Zinc protease]] | ||