1cxq

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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=1cxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cxq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cxq RCSB], [http://www.ebi.ac.uk/pdbsum/1cxq 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=1cxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cxq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cxq RCSB], [http://www.ebi.ac.uk/pdbsum/1cxq PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/POL_RSVP POL_RSVP]] Capsid protein p27 forms the spherical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 05:06, 25 December 2014

ATOMIC RESOLUTION ASV INTEGRASE CORE DOMAIN FROM AMMONIUM SULFATE

1cxq, resolution 1.02Å

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