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7TB9

Structural characterization of the biological synthetic peptide pCEMP1

Summary for 7TB9
Entry DOI10.2210/pdb7tb9/pdb
NMR InformationBMRB: 30978
DescriptorCEMP1-p1 (1 entity in total)
Functional Keywordsde novo protein
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight2114.22
Authors
Lopez Giraldo, A.,del Rio Portilla, F.,Nidome Campos, M.,Romo Arevalo, E.,Arzate, H. (deposition date: 2021-12-21, release date: 2023-01-18, Last modification date: 2024-05-15)
Primary citationCampos, M.N.,Giraldo, E.L.,Del Rio Portilla, F.,Fernandez-Velasco, D.A.,Arzate, H.,Romo-Arevalo, E.
Solution NMR structure of cementum protein 1 derived peptide (CEMP1-p1) and its role in the mineralization process.
J.Pept.Sci., 29:e3494-e3494, 2023
Cited by
PubMed Abstract: We report the characterization of the three-dimensional structure of the CEMP1-p1 peptide [MGTSSTDSQQAQHRRCSTSN: corresponding to residues 1-20 of the N-terminus of cementum protein 1 (CEMP1)]. This peptide imitates the capacity of CEMP1 to stimulate hydroxyapatite (HA) crystal nucleation and growth, and promotes the differentiation of periodontal ligament cells into a cementoblastic phenotype. Additionally, in experimental models of critical-sized calvarial defects in Wistar rats, CEMP1-p1 has shown osteogenic properties that enhanced the physiological deposition and maturation of newly formed bone. In this work, studies of CEMP1-p1 by circular dichroism (CD) and nuclear magnetic resonance (NMR) were performed in trifluoroethanol D2 (TFED2) and aqueous solution to determine the 3D structure of the peptide. Using the 3D model, experimental data from HA crystals formation and calcium fluorescence emission, we explain the biological mechanisms involved in CEMP1-p1 activity to promote calcium recruitment and its affinity to HA crystals. This information is valuable because it proposes, for the first time, a plausible molecular mechanism during the mineralization process, from a specific cementum protein-derived peptide.
PubMed: 37051739
DOI: 10.1002/psc.3494
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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