1q8h

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(New page: 200px<br /><applet load="1q8h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q8h, resolution 2.00&Aring;" /> '''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"
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[[Image:1q8h.jpg|left|200px]]<br /><applet load="1q8h" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1q8h, resolution 2.00&Aring;" />
caption="1q8h, resolution 2.00&Aring;" />
'''Crystal structure of porcine osteocalcin'''<br />
'''Crystal structure of porcine osteocalcin'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1Q8H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q8H OCA].
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1Q8H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q8H OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Hoang, Q.Q.]]
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[[Category: Hoang, Q Q.]]
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[[Category: Howard, A.J.]]
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[[Category: Howard, A J.]]
[[Category: Sicheri, F.]]
[[Category: Sicheri, F.]]
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[[Category: Yang, D.S.]]
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[[Category: Yang, D S.]]
[[Category: CA]]
[[Category: CA]]
[[Category: bone gla protein]]
[[Category: bone gla protein]]
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[[Category: paper-clip]]
[[Category: paper-clip]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:29:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:11 2008''

Revision as of 12:37, 21 February 2008


1q8h, resolution 2.00Å

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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 with as ligand. 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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