1gnh: Difference between revisions
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==HUMAN C-REACTIVE PROTEIN== | ==HUMAN C-REACTIVE PROTEIN== | ||
<StructureSection load='1gnh' size='340' side='right' caption='[[1gnh]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1gnh' size='340' side='right' caption='[[1gnh]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
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<table><tr><td colspan='2'>[[1gnh]] 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=1GNH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GNH FirstGlance]. <br> | <table><tr><td colspan='2'>[[1gnh]] 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=1GNH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GNH FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1gnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gnh OCA], [http://pdbe.org/1gnh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gnh RCSB], [http://www.ebi.ac.uk/pdbsum/1gnh 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=1gnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gnh OCA], [http://pdbe.org/1gnh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gnh RCSB], [http://www.ebi.ac.uk/pdbsum/1gnh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gnh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gn/1gnh_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gn/1gnh_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 09:30, 3 January 2018
HUMAN C-REACTIVE PROTEINHUMAN C-REACTIVE PROTEIN
Structural highlights
Function[CRP_HUMAN] Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of the classical acute phase reactant human C-reactive protein provides evidence that phosphocholine binding is mediated through calcium and a hydrophobic pocket centred on Phe 66. The residue Glu 81 is suitably positioned to interact with the choline group. A cleft on the pentameric face opposite to that containing the calcium site may have an important functional role. The structure provides insights into the molecular mechanisms by which this highly conserved plasma protein, for which no polymorphism or deficiency state is known, may exert its biological role. Three dimensional structure of human C-reactive protein.,Shrive AK, Cheetham GM, Holden D, Myles DA, Turnell WG, Volanakis JE, Pepys MB, Bloomer AC, Greenhough TJ Nat Struct Biol. 1996 Apr;3(4):346-54. PMID:8599761[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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