Phosphorylation regulates the secondary structure and function of dentin phosphoprotein peptides

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• 作者：Eduardo Villarreal-Ramirez^a ; ^d ; ¹ ; David Eliezer^b ; Ramon Garduñ ; o-Juarez^c ; Arne Gericke^d ; Jose Manuel Perez-Aguilar^e ; Adele Boskey^a ; ^f ; ^{boskeya@hss.edu}
• 关键词：DPP ; dentin phosphoprotein ; NCPs ; non collagen proteins ; IDPs ; intrinsically disordered proteins ; HA ; hydroxyapatite ; CK2 ; casein kinase 2 ; SAXS ; small angle X-ray scattering ; FTIR ; Fourier transform infrared spectroscopy
• 刊名：Bone
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：95
• 期：Complete
• 页码：65-75
• 全文大小：1123 K
• 卷排序：95

文摘

Dentin phosphophoryn (DPP) binding to hydroxyapatite mineral (HA) was modeled using molecular dynamics (MD) simulations. Average structure of DPP peptides, in water or adsorbed onto HA surface, is modulated by their phosphorylation. One peptide, P5 and its phosphorylated form P5P, the most frequently occurring in DPP, varied in flexibility in a phosphorylation-dependent manner. The peptide’s secondary structure is controlled by phosphorylation of a serine residue located at the third position in the triplet motif DSS. Solution studies showed this phosphorylated peptide promotes HA crystal growth, whereas the unphosphorylated peptide inhibits HA crystal growth.