View source for 4aig


==ADAMALYSIN II WITH PHOSPHONATE INHIBITOR==
<StructureSection load='4aig' size='340' side='right'caption='[[4aig]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4aig]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4AIG 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></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=4aig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aig OCA], [https://pdbe.org/4aig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aig RCSB], [https://www.ebi.ac.uk/pdbsum/4aig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aig ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VM12_CROAD VM12_CROAD] Has no significant hemorrhagic activity, but inactivates serpins by limited proteolysis of their reactive-site loops.
== 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/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=4aig ConSurf].
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4aig" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Crotalus adamanteus]]
[[Category: Large Structures]]
[[Category: Cirilli M]]
[[Category: Gavuzzo E]]
[[Category: Mazza F]]
[[Category: Pochetti G]]