1lj7: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1lj7.png|left|200px]]
-<!--
+==Crystal structure of calcium-depleted human C-reactive protein from perfectly twinned data==
-The line below this paragraph, containing "STRUCTURE_1lj7", creates the "Structure Box" on the page.
+<StructureSection load='1lj7' size='340' side='right'caption='[[1lj7]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1lj7]] 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=1LJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LJ7 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.15&#8491;</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=1lj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lj7 OCA], [https://pdbe.org/1lj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lj7 RCSB], [https://www.ebi.ac.uk/pdbsum/1lj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lj7 ProSAT]</span></td></tr>
-{{STRUCTURE_1lj7|  PDB=1lj7  |  SCENE=  }}
+</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/lj/1lj7_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=1lj7 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+C-reactive protein is a member of the pentraxin family of oligomeric serum proteins which has been conserved through evolution, homologues having been found in every species in which they have been sought. Human C-reactive protein (hCRP) is the classical acute-phase reactant produced in large amounts in response to tissue damage and inflammation and is used almost universally as a clinical indicator of infection and inflammation. The role of hCRP in host defence and the calcium-dependent ligand-binding specificity of hCRP for phosphocholine moieties have long been recognized. In order to clarify the structural rearrangements associated with calcium binding, the reported affinity of calcium-depleted hCRP for polycations and other ligands, and the role of calcium in protection against denaturation and proteolysis, the structure of calcium-depleted hCRP has been determined by X-ray crystallography. Crystals of calcium-depleted hCRP are invariably twinned and those suitable for analysis are merohedral type II twins of point group 4 single crystals. The structure has been solved by molecular replacement using the calcium-bound hCRP structure [Shrive et al. (1996), Nature Struct. Biol. 3, 346-354]. It reveals two independent pentamers which form a face-to-face decamer across a dyad near-parallel to the twinning twofold axis. Cycles of intensity deconvolution, density modification (tenfold NCS) and model building, eventually including refinement, give a final R factor of 0.19 (R(free) = 0.20). Despite poor definition in some areas arising from the limited resolution of the data and from the twinning and disorder, the structure reveals the probable mode of twinning and the conformational changes, localized in one of the calcium-binding loops, which accompany calcium binding.
-===Crystal structure of calcium-depleted human C-reactive protein from perfectly twinned data===
+The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals.,Ramadan MA, Shrive AK, Holden D, Myles DA, Volanakis JE, DeLucas LJ, Greenhough TJ Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):992-1001. Epub, 2002 May 29. PMID:12037301<ref>PMID:12037301</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1lj7" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_12037301}}, adds the Publication Abstract to the page
+*[[C-reactive protein|C-reactive protein]]
-(as it appears on PubMed at http://www.pubmed.gov), where 12037301 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_12037301}}
+__TOC__
+</StructureSection>
-==About this Structure==
-LJ7 is a [[Single protein]] structure of 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=1LJ7 OCA].
-==Reference==
-The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals., Ramadan MA, Shrive AK, Holden D, Myles DA, Volanakis JE, DeLucas LJ, Greenhough TJ, Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):992-1001. Epub, 2002 May 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12037301 12037301]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: DeLucas, L J.]]
+[[Category: DeLucas LJ]]
-[[Category: Greenhough, T J.]]
+[[Category: Greenhough TJ]]
-[[Category: Holden, D.]]
+[[Category: Holden D]]
-[[Category: Myles, D A.]]
+[[Category: Myles DA]]
-[[Category: Ramadan, M A.]]
+[[Category: Ramadan MA]]
-[[Category: Shrive, A K.]]
+[[Category: Shrive AK]]
-[[Category: Volanakis, J E.]]
+[[Category: Volanakis JE]]
-[[Category: Decamer]]
-[[Category: Pentamer]]
-[[Category: Pentraxin fold]]
-[[Category: Twinned]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 21:00:40 2008''