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| - | | + | #REDIRECT [[6tav]] This PDB entry is obsolete and replaced by 6tav |
| - | ==Alpha-2 Macroglobulin==
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| - | <StructureSection load='4acq' size='340' side='right'caption='[[4acq]], [[Resolution|resolution]] 4.30Å' scene=''>
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| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[4acq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ACQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4ACQ FirstGlance]. <br>
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| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
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| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MEQ:N5-METHYLGLUTAMINE'>MEQ</scene></td></tr>
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| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bv8|1bv8]]</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4acq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4acq OCA], [http://pdbe.org/4acq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4acq RCSB], [http://www.ebi.ac.uk/pdbsum/4acq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4acq ProSAT]</span></td></tr>
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| - | </table>
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| - | == Function ==
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| - | [[http://www.uniprot.org/uniprot/A2MG_HUMAN A2MG_HUMAN]] Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.
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| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | I'm your Venus: The crystal structure of the human methylamine-induced form of alpha(2) -macroglobulin (alpha(2) M) shows its large central cavity can accommodate two medium-sized proteinases (see structure, front part clipped off to better show central cavity). Twelve major entrances provide access for small substrates to the cavity and the still-active trapped "prey". The structure unveils the molecular basis of the unique "venus flytrap" mechanism of alpha(2) M.
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| - | The Crystal Structure of Human alpha(2) -Macroglobulin Reveals a Unique Molecular Cage.,Marrero A, Duquerroy S, Trapani S, Goulas T, Guevara T, Andersen GR, Navaza J, Sottrup-Jensen L, Gomis-Ruth FX Angew Chem Int Ed Engl. 2012 Jan 31. doi: 10.1002/anie.201108015. PMID:22290936<ref>PMID:22290936</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4acq" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| - | __TOC__
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| - | </StructureSection>
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| - | [[Category: Homo sapiens]]
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| - | [[Category: Large Structures]]
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| - | [[Category: Andersen, G R]]
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| - | [[Category: Duquerroy, S]]
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| - | [[Category: Gomis-Ruth, F X]]
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| - | [[Category: Goulas, T]]
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| - | [[Category: Guevara, T]]
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| - | [[Category: Marrero, A]]
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| - | [[Category: Navaza, J]]
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| - | [[Category: Sottrup-Jensen, L]]
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| - | [[Category: Trapani, S]]
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| - | [[Category: Blood plasma inhibitor]]
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| - | [[Category: Conformational change]]
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| - | [[Category: Hydrolase inhibitor]]
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| - | [[Category: Irreversible proteinase inhibitor]]
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| - | [[Category: Proteinase inhibitor]]
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