1q8h

From Proteopedia

(Difference between revisions)

Revision as of 08:59, 21 April 2021

Crystal structure of porcine osteocalcin

Structural highlights

1q8h is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[OSTCN_PIG] Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium.

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hoang QQ, Sicheri F, Howard AJ, Yang DS. Bone recognition mechanism of porcine osteocalcin from crystal structure. Nature. 2003 Oct 30;425(6961):977-80. PMID:14586470 doi:10.1038/nature02079

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q8h"

@@ Line 3: / Line 3: @@
 <StructureSection load='1q8h' size='340' side='right'caption='[[1q8h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1q8h]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q8H FirstGlance]. <br>
+<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='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" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q8h OCA], [http://pdbe.org/1q8h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q8h RCSB], [http://www.ebi.ac.uk/pdbsum/1q8h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q8h ProSAT]</span></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 ==
-[[http://www.uniprot.org/uniprot/OSTCN_PIG OSTCN_PIG]] Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium.
+[[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]]

1q8h

From Proteopedia

Revision as of 08:59, 21 April 2021

Crystal structure of porcine osteocalcin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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