1gnh: Difference between revisions

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New page: left|200px<br /> <applet load="1gnh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gnh, resolution 3.0Å" /> '''HUMAN C-REACTIVE PRO...
 
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[[Image:1gnh.gif|left|200px]]<br />
<applet load="1gnh" size="450" color="white" frame="true" align="right" spinBox="true"
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'''HUMAN C-REACTIVE PROTEIN'''<br />


==Overview==
==HUMAN C-REACTIVE PROTEIN==
The 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.
<StructureSection load='1gnh' size='340' side='right'caption='[[1gnh]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gnh]] is a 10 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1GNH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=1gnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gnh OCA], [https://pdbe.org/1gnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gnh RCSB], [https://www.ebi.ac.uk/pdbsum/1gnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gnh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CRP_HUMAN 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gnh ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known disease associated with this structure: Specific granule deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600749 600749]]
*[[C-reactive protein|C-reactive protein]]
 
__TOC__
==About this Structure==
</StructureSection>
1GNH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GNH OCA].
 
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8599761 8599761]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bloomer, A.C.]]
[[Category: Bloomer AC]]
[[Category: Cheetham, G.M.T.]]
[[Category: Cheetham GMT]]
[[Category: Greenhough, T.J.]]
[[Category: Greenhough TJ]]
[[Category: Holden, D.]]
[[Category: Holden D]]
[[Category: Myles, D.A.]]
[[Category: Myles DA]]
[[Category: Pepys, M.B.]]
[[Category: Pepys MB]]
[[Category: Shrive, A.K.]]
[[Category: Shrive AK]]
[[Category: Turnell, W.G.]]
[[Category: Turnell WG]]
[[Category: Volanakis, J.E.]]
[[Category: Volanakis JE]]
[[Category: CA]]
[[Category: acute-phase protein]]
[[Category: acute-phase reactant]]
[[Category: pentraxin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:07:15 2007''

Latest revision as of 14:22, 27 March 2024

HUMAN C-REACTIVE PROTEINHUMAN C-REACTIVE PROTEIN

Structural highlights

1gnh is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

1gnh, resolution 3.00Å

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