4avt
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4avt]] is a 10 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=4AVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AVT FirstGlance]. <br> | <table><tr><td colspan='2'>[[4avt]] is a 10 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=4AVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AVT FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GHE:(2R)-1-[6-[(2R)-2-CARBOXYPYRROLIDIN-1-YL]-6-OXIDANYLIDENE-HEXANOYL]PYRROLIDINE-2-CARBOXYLIC+ACID'>GHE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GHE:(2R)-1-[6-[(2R)-2-CARBOXYPYRROLIDIN-1-YL]-6-OXIDANYLIDENE-HEXANOYL]PYRROLIDINE-2-CARBOXYLIC+ACID'>GHE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gyk|1gyk]], [[1lgn|1lgn]], [[1sac|1sac]], [[2a3w|2a3w]], [[2a3x|2a3x]], [[2a3y|2a3y]], [[2w08|2w08]], [[4avs|4avs]], [[4avv|4avv]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gyk|1gyk]], [[1lgn|1lgn]], [[1sac|1sac]], [[2a3w|2a3w]], [[2a3x|2a3x]], [[2a3y|2a3y]], [[2w08|2w08]], [[4avs|4avs]], [[4avv|4avv]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4avt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4avt RCSB], [http://www.ebi.ac.uk/pdbsum/4avt 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=4avt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4avt RCSB], [http://www.ebi.ac.uk/pdbsum/4avt PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
== Disease == | == Disease == | ||
[[http://www.uniprot.org/uniprot/SAMP_HUMAN SAMP_HUMAN]] Note=SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits. | [[http://www.uniprot.org/uniprot/SAMP_HUMAN SAMP_HUMAN]] Note=SAP is a precursor of amyloid component P which is found in basement membrane and associated with amyloid deposits. | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/SAMP_HUMAN SAMP_HUMAN]] Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin. | [[http://www.uniprot.org/uniprot/SAMP_HUMAN SAMP_HUMAN]] Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Under physiological conditions, the pentameric human plasma protein serum amyloid P component (SAP) binds hexanoyl bis(D-proline) (R-1-{6-[R-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl}pyrrolidine-2-carboxylic acid; CPHPC) through its D-proline head groups in a calcium-dependent interaction. Cooperative effects in binding lead to a substantial enhancement of affinity. Five molecules of the bivalent ligand cross-link and stabilize pairs of SAP molecules, forming a decameric complex that is rapidly cleared from the circulation by the liver. Here, it is reported that X-ray analysis of the SAP complex with CPHPC and cadmium ions provides higher resolution detail of the interaction than is observed with calcium ions. Conformational isomers of CPHPC observed in solution by HPLC and by X-ray analysis are compared with the protein-bound form. These are discussed in relation to the development of CPHPC to provide SAP depletion for the treatment of amyloidosis and other indications. | ||
| + | |||
| + | Interaction of serum amyloid P component with hexanoyl bis(D-proline) (CPHPC).,Kolstoe SE, Jenvey MC, Purvis A, Light ME, Thompson D, Hughes P, Pepys MB, Wood SP Acta Crystallogr D Biol Crystallogr. 2014 Aug 1;70(Pt 8):2232-40. doi:, 10.1107/S1399004714013455. Epub 2014 Jul 25. PMID:25084341<ref>PMID:25084341</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:56, 22 October 2014
Structure of CPHPC bound to Serum Amyloid P Component
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