Bone recognition mechanism of porcine osteocalcin from crystal structure

Quyen Q. Hoang, Frank Sicheri, Andrew J. Howard, Daniel S.C. Yang

Research output: Contribution to journalArticle

389 Scopus citations

Abstract

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 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.

Original languageEnglish (US)
Pages (from-to)977-980
Number of pages4
JournalNature
Volume425
Issue number6961
DOIs
StatePublished - Oct 30 2003
Externally publishedYes

ASJC Scopus subject areas

  • General

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