Document Detail


Delineation of conformational preferences in human salivary statherin by 1H, 31P NMR and CD studies: sequential assignment and structure-function correlations.
MedLine Citation:
PMID:  9745898     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Membrane-induced solution structure of human salivary statherin, a 43 amino acid residue acidic phosphoprotein, has been investigated by two-dimensional proton nuclear magnetic resonance (2D 1H NMR) spectroscopy. NMR assignments and structural analysis of this phosphoprotein was accomplished by analyzing the pattern of sequential and medium range NOEs, alphaCH chemical shift perturbations and deuterium exchange measurements of the amide proton resonances. The NMR data revealed three distinct structural motifs in the molecule: (1) an alpha-helical structure at the N-terminal domain comprising Asp1-Tyr16, (2) a polyproline type II (PPII) conformation predominantly occurring at the middle proline-rich domain spanning Gly19-Gln35, and (3) a 3(10)-helical structure at the C-terminal Pro36-Phe43 sequence. Presence of a few weak dalphaN(i,i+2) NOEs suggests that N-terminus also possesses minor population of 3(10)-helical conformation. Of the three secondary structural elements, helical structure formed by the N-terminal residues, Asp1-Ile11 appears to be more rigid as observed by the relatively very slow exchange of amide hydrogens of Glu5-Ile11. 31P NMR experiments clearly indicated that N-terminal domain of statherin exists mainly in disordered state in water whereas, upon addition of structure stabilizing co-solvent, 2,2,2-trifluorethanol (TFE), it showed a strong propensity for helical conformation. Calcium ion interaction studies suggested that the disordered N-terminal region encompassing the two vicinal phosphoserines is essential for the binding of calcium ions in vivo. Results from the circular dichroism (CD) experiments were found to be consistent with and complimentary to the NMR data and provided an evidence that non-aqueous environment such as TFE, could induce the protein to fold into helical conformation. The findings that the statherin possesses blended solvent sensitive secondary structural elements and the requirement of non-structured N-terminal region under aqueous environment in calcium ion interaction may be invaluable to understand various physiological functions of statherin in the oral fluid.
Authors:
G A Naganagowda; T L Gururaja; M J Levine
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of biomolecular structure & dynamics     Volume:  16     ISSN:  0739-1102     ISO Abbreviation:  J. Biomol. Struct. Dyn.     Publication Date:  1998 Aug 
Date Detail:
Created Date:  1999-01-12     Completed Date:  1999-01-12     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  8404176     Medline TA:  J Biomol Struct Dyn     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  91-107     Citation Subset:  IM    
Affiliation:
Department of Oral Biology and Dental Research Institute, State University of New York at Buffalo, 14214-3092, USA.
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MeSH Terms
Descriptor/Qualifier:
Calcium / metabolism
Circular Dichroism*
Humans
Hydrogen
Ions
Molecular Conformation*
Nuclear Magnetic Resonance, Biomolecular* / methods
Phosphorus Radioisotopes
Protein Structure, Secondary
Salivary Glands / chemistry*
Salivary Proteins and Peptides / chemistry*,  metabolism
Structure-Activity Relationship
Grant Support
ID/Acronym/Agency:
DE08240/DE/NIDCR NIH HHS; DEO7585/DE/NIDCR NIH HHS
Chemical
Reg. No./Substance:
0/Ions; 0/Phosphorus Radioisotopes; 0/STATH protein, human; 0/Salivary Proteins and Peptides; 1333-74-0/Hydrogen; 7440-70-2/Calcium

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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