Partial high-resolution structure of phosphorylated and non-phosphorylated leucine-rich amelogenin protein adsorbed to hydroxyapatite

Journal Article · Thu Jul 21 04:00:00 EDT 2011 · Journal of Physical Chemistry C, 115(28):13775-13785

DOI:https://doi.org/10.1021/jp202965h· OSTI ID:1021825

Masica, David L; Gray, Jeffrey J; Shaw, Wendy J

The formation of biogenic materials requires the interaction of organic molecules with the mineral phase. In forming enamel, the amelogenin proteins contribute to the mineralization of hydroxyapatite (HAp). Leucine-rich amelogenin protein (LRAP) is a naturally occurring splice variant of amelogenin that comprises amelogenin’s predicted HAp binding domains. We determined the partial structure of phosphorylated and non-phosphorylated LRAP variants bound to HAp using combined solid-state NMR (ssNMR) and ssNMR-biased computational structure prediction. The ssNMR measurements indicate a largely extended structure for both variants, though some measurements are consistent with a partially helical N-terminal segment. Structure prediction was biased using 21 ssNMR measurements at five HAp crystal faces. The predicted fold of LRAP is similar at all HAp faces studied, regardless of phosphorylation. LRAP’s predicted structure is relatively extended with a helix-turn-helix motif in the N-terminal domain and some helix in the C-terminal domain. The N-terminal domain of the phosphorylated variant binds HAp more tightly than the N-terminal domain of the non-phosphorylated variant. Both variants are predicted to preferentially bind the {010} HAp crystal face providing further evidence that amelogenins block crystal growth on the a and b faces to allow elongated crystals in the c-axis. Pacific Northwest National Laboratory is operated by Battelle for the US Department of Energy.

• Research Organization: Pacific Northwest National Laboratory (PNNL), Richland, WA (US)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC05-76RL01830
• OSTI ID: 1021825
• Report Number(s): PNNL-SA-78683; 400412000
• Journal Information: Journal of Physical Chemistry C, 115(28):13775-13785, Journal Name: Journal of Physical Chemistry C, 115(28):13775-13785 Journal Issue: 28 Vol. 115; ISSN 1932-7447
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS
Amelogenin
Biomineralization
CRYSTAL GROWTH
FORECASTING
LRAP
MINERALIZATION
PHOSPHORYLATION
PROTEINS
RosettaSurface
Solid-state NMR