1q8h
From Proteopedia
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| - | [[Image:1q8h.jpg|left|200px]] | + | [[Image:1q8h.jpg|left|200px]] |
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| - | '''Crystal structure of porcine osteocalcin''' | + | {{Structure |
| + | |PDB= 1q8h |SIZE=350|CAPTION= <scene name='initialview01'>1q8h</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of porcine osteocalcin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Q8H is a [ | + | 1Q8H is a [[Single protein]] structure of 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]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14586470 14586470] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: paper-clip]] | [[Category: paper-clip]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:34:20 2008'' |
Revision as of 11:34, 20 March 2008
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| , resolution 2.00Å | |||||||
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| 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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