1dp5
From Proteopedia
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<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=1dp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dp5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dp5 RCSB], [http://www.ebi.ac.uk/pdbsum/1dp5 PDBsum]</span></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=1dp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dp5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dp5 RCSB], [http://www.ebi.ac.uk/pdbsum/1dp5 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/CARP_YEAST CARP_YEAST]] Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself. [[http://www.uniprot.org/uniprot/IPA3_YEAST IPA3_YEAST]] Specific and potent inhibitor for yeast aspartic protease A (yscA). The proteinase acts as a folding template stabilizing the helical conformation in the inhibitor, which results in the potent and specific blockage of the proteolytic activity. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 21:02, 25 December 2014
THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR
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