1edy

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<StructureSection load='1edy' size='340' side='right'caption='[[1edy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1edy' size='340' side='right'caption='[[1edy]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1edy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EDY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1edy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EDY FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1edy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edy OCA], [http://pdbe.org/1edy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1edy RCSB], [http://www.ebi.ac.uk/pdbsum/1edy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1edy ProSAT]</span></td></tr>
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</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=1edy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edy OCA], [https://pdbe.org/1edy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1edy RCSB], [https://www.ebi.ac.uk/pdbsum/1edy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1edy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/A1M_RAT A1M_RAT]] 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 (By similarity).[UniProtKB:P01023]
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[[https://www.uniprot.org/uniprot/A1M_RAT A1M_RAT]] 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 (By similarity).[UniProtKB:P01023]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 09:36, 21 July 2021

CRYSTAL STRUCTURE OF RAT ALPHA 1-MACROGLOBULIN RECEPTOR BINDING DOMAIN

PDB ID 1edy

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