1q8h
From Proteopedia
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|PDB= 1q8h |SIZE=350|CAPTION= <scene name='initialview01'>1q8h</scene>, resolution 2.00Å | |PDB= 1q8h |SIZE=350|CAPTION= <scene name='initialview01'>1q8h</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>, <scene name='pdbligand=X:2'-DEOXY-N7-(8,9-DIHYDRO-9-HYDROXY-10-DEHYDROXY-AFLATOXIN)GUANOSINE+MONOPHOSPHATE'>X</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/1q8h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q8h RCSB]</span> | ||
}} | }} | ||
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[[Category: Sicheri, F.]] | [[Category: Sicheri, F.]] | ||
[[Category: Yang, D S.]] | [[Category: Yang, D S.]] | ||
| - | [[Category: CA]] | ||
[[Category: bone gla protein]] | [[Category: bone gla protein]] | ||
[[Category: calcium binding protein]] | [[Category: calcium binding protein]] | ||
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[[Category: paper-clip]] | [[Category: paper-clip]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:10:12 2008'' |
Revision as of 20:10, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of porcine osteocalcin
Overview
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.
About this Structure
1Q8H is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
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
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