Bone recognition mechanism of porcine osteocalcin from crystal structure

Quyen Q. Hoang, Frank Sicheri, Andrew J. Howard and Daniel S. C. Yang ()
Additional contact information
Quyen Q. Hoang: Faculty of Health Science, McMaster University
Frank Sicheri: Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital
Andrew J. Howard: Chemical and Physical Sciences, Illinois Institute Technology
Daniel S. C. Yang: Faculty of Health Science, McMaster University

Nature, 2003, vol. 425, issue 6961, 977-980

Abstract: Abstract Osteocalcin is the most abundant noncollagenous protein in bone1, and its concentration in serum is closely linked to bone metabolism and serves as a biological marker for the clinical assessment of bone disease2. Although its precise mechanism of action is unclear, osteocalcin influences bone mineralization3,4, in part through its ability to bind with high affinity to the mineral component of bone, hydroxyapatite5. In addition to binding to hydroxyapatite, osteocalcin functions in cell signalling and the recruitment of osteoclasts6 and osteoblasts7, which have active roles in bone resorption and deposition, respectively. Here we present the X-ray crystal structure of porcine osteocalcin at 2.0 Å 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.

Date: 2003
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature02079 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:425:y:2003:i:6961:d:10.1038_nature02079

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature02079

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().