ArticleThe journal of physical chemistry. B2008
Structure, orientation, and dynamics of the C-terminal hexapeptide of LRAP determined using solid-state NMR.
Article in The journal of physical chemistry. B, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Review
- A N-Terminus Domain Determines Amelogenin's Stability to Guide the Development of Mouse Enamel Matrix.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2021Article
- Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite.Journal of structural biology · 2020Review
- Meeting report: a hard look at the state of enamel research.International journal of oral science · 2017Article
- Phosphorylation regulates the secondary structure and function of dentin phosphoprotein peptides.Bone · 2017Article
- Protein Phosphorylation and Mineral Binding Affect the Secondary Structure of the Leucine-Rich Amelogenin Peptide.Frontiers in physiology · 2017Article
- Solid-state NMR studies of proteins immobilized on inorganic surfaces.Solid state nuclear magnetic resonance · 2015Review
- The flexible structure of the K24S28 region of Leucine-Rich Amelogenin Protein (LRAP) bound to apatites as a function of surface type, calcium, mutation, and ionic strength.Frontiers in physiology · 2014Article
- Mineral association changes the secondary structure and dynamics of murine amelogenin.Journal of dental research · 2013Article
- Phosphorylation and ionic strength alter the LRAP-HAP interface in the N-terminus.Biochemistry · 2013Article
- Neutron reflectometry studies of the adsorbed structure of the amelogenin, LRAP.The journal of physical chemistry. B · 2013Article
- Biophysical characterization of synthetic amelogenin C-terminal peptides.European journal of oral sciences · 2012Article
- Effect of phosphorylation on the interaction of calcium with leucine-rich amelogenin peptide.European journal of oral sciences · 2011Article
- Single-molecule determination of the face-specific adsorption of Amelogenin's C-terminus on hydroxyapatite.Angewandte Chemie (International ed. in English) · 2011Article
- Partial high-resolution structure of phosphorylated and non-phosphorylated leucine-rich amelogenin protein adsorbed to hydroxyapatite.The journal of physical chemistry. C, Nanomaterials and interfaces · 2011Article
- Binding of glycosaminoglycan saccharides to hydroxyapatite surfaces: A density functional theory study.Proceedings. Mathematical, physical, and engineering sciences · 2011Article
- Potential role of the amelogenin N-terminus in the regulation of calcium phosphate formation in vitro.Cells, tissues, organs · 2011Article
- A solution NMR investigation into the murine amelogenin splice-variant LRAP (Leucine-Rich Amelogenin Protein).Biochimica et biophysica acta · 2010Article
- The leucine rich amelogenin protein (LRAP) adsorbs as monomers or dimers onto surfaces.Journal of structural biology · 2010Article
- Amelogenin nanoparticles in suspension: deviations from spherical shape and pH-dependent aggregation.Biomacromolecules · 2010Article
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2 authors.
Funding
Abstract
Amelogenin is the predominant protein found during enamel development and has been shown to be essential to proper enamel formation. Leucine-rich amelogenin peptide (LRAP) is a naturally occurring splice variant that preserves the charged N- and C-termini of full length amelogenin, regions thought to be crucial in interacting with hydroxaypatite. Particularly, the highly charged C-terminal hexapeptide (KREEVD) is thought to be the region most intimately interacting with hydroxyapatite (HAP). The structure of this charged region was investigated, along with the proximity to the surface and the mobility of two of the residues. The structure was found to be consistent with a random coil or more extended structure, as has been seen for more internalized residues in the C-terminus. The backbone K54(13C'), V58(13C'), and V58(15N) were all found to be close to the surface of HAP, approximately 6.0 angstroms from the nearest 31P atom, suggesting a strong interaction and emphasizing the importance of these residues in interacting with HAP. However, both ends of the hexapeptide at residues K54 and V58 experience significant mobility under hydrated conditions, implying that another portion of the protein helps to stabilize the strong LRAP-HAP interaction. Interestingly, the backbone of the C-terminal third of the protein is consistently 6.0 angstroms from the HAP surface, providing a model in this region of the protein lying flat on the surface with no three-dimensional folding. The combination of these features, that is, a random coil structure, a significant mobility, and a lack of three-dimensional folding in this region of the protein, may have an important functional role, possibly allowing maximum crystal inhibition at low protein concentrations.
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