1q8h
From Proteopedia
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(New page: 200px<br /><applet load="1q8h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q8h, resolution 2.00Å" /> '''Crystal structure of...) |
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- | [[Image:1q8h.jpg|left|200px]]<br /><applet load="1q8h" size="450" color="white" frame="true" align="right" spinBox="true" | ||
- | caption="1q8h, resolution 2.00Å" /> | ||
- | '''Crystal structure of porcine osteocalcin'''<br /> | ||
- | == | + | ==Crystal structure of porcine osteocalcin== |
- | Osteocalcin is the most abundant noncollagenous protein in bone, and its | + | <StructureSection load='1q8h' size='340' side='right'caption='[[1q8h]], [[Resolution|resolution]] 2.00Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1q8h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q8H 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]] 2Å</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>, <scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</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=1q8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8h OCA], [https://pdbe.org/1q8h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q8h RCSB], [https://www.ebi.ac.uk/pdbsum/1q8h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q8h ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/OSTCN_PIG OSTCN_PIG] Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium. | ||
+ | == 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/q8/1q8h_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1q8h ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Osteocalcin is the most abundant noncollagenous protein in bone, and its concentration in serum is closely linked to bone metabolism and serves as a biological marker for the clinical assessment of bone disease. Although its precise mechanism of action is unclear, osteocalcin influences bone mineralization, in part through its ability to bind with high affinity to the mineral component of bone, hydroxyapatite. In addition to binding to hydroxyapatite, osteocalcin functions in cell signalling and the recruitment of osteoclasts and osteoblasts, which have active roles in bone resorption and deposition, respectively. Here we present the X-ray crystal structure of porcine osteocalcin at 2.0 A resolution, which reveals a negatively charged protein surface that coordinates five calcium ions in a spatial orientation that is complementary to calcium ions in a hydroxyapatite crystal lattice. On the basis of our findings, we propose a model of osteocalcin binding to hydroxyapatite and draw parallels with other proteins that engage crystal lattices. | ||
- | + | Bone recognition mechanism of porcine osteocalcin from crystal structure.,Hoang QQ, Sicheri F, Howard AJ, Yang DS Nature. 2003 Oct 30;425(6961):977-80. PMID:14586470<ref>PMID:14586470</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | [[Category: | + | <div class="pdbe-citations 1q8h" style="background-color:#fffaf0;"></div> |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
- | [[Category: Hoang | + | [[Category: Hoang QQ]] |
- | [[Category: Howard | + | [[Category: Howard AJ]] |
- | [[Category: Sicheri | + | [[Category: Sicheri F]] |
- | [[Category: Yang | + | [[Category: Yang DS]] |
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Current revision
Crystal structure of porcine osteocalcin
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