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Bone recognition mechanism of porcine osteocalcin from crystal structure
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Bone recognition mechanism of porcine osteocalcin from crystal structure
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Journal Article
Bone recognition mechanism of porcine osteocalcin from crystal structure
2003
Overview
Osteocalcin is the most abundant noncollagenous protein in bone
1
, and its concentration in serum is closely linked to bone metabolism and serves as a biological marker for the clinical assessment of bone disease
2
. Although its precise mechanism of action is unclear, osteocalcin influences bone mineralization
3
,
4
, in part through its ability to bind with high affinity to the mineral component of bone, hydroxyapatite
5
. In addition to binding to hydroxyapatite, osteocalcin functions in cell signalling and the recruitment of osteoclasts
6
and osteoblasts
7
, 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.
Publisher
Nature Publishing Group UK,Nature Publishing,Nature Publishing Group
Subject
/ Biological and medical sciences
/ Bones
/ Calcium
/ Crystals
/ Diseases of the osteoarticular system
/ Fundamental and applied biological sciences. Psychology
/ Humanities and Social Sciences
/ Ions
/ letter
/ Miscellaneous. Osteoarticular involvement in other diseases
/ Protein Structure, Secondary
/ Proteins
/ Science
/ Structure-Activity Relationship
/ Swine
/ Vertebrates: osteoarticular system, musculoskeletal system
