NDLI: Identification of the amino acids comprising a surface-exposed epitope within the nucleotide-binding domain of the Na+,K(+)-ATPase using a random peptide library.

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Sequence-specific 1H-NMR assignments and folding topology of human CD59.

Thermodynamics of BPTI folding.

Identification of the amino acids comprising a surface-exposed epitope within the nucleotide-binding domain of the Na+,K(+)-ATPase using a random peptide library.

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Identification of the amino acids comprising a surface-exposed epitope within the nucleotide-binding domain of the Na+,K(+)-ATPase using a random peptide library.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ball, W. J. Malik, B. Jamieson, G. A.
Description	Author Affiliation: Malik B ( Department of Pharmacology and Cell Biophysics, College of Medicine, University of Cincinnati, Ohio 45267-0575.)
Abstract	Monoclonal antibodies that bind native protein can generate considerable information about structure/function relationships, but identification of their epitopes can be problematic. Previously, monoclonal antibody M8-P1-A3 has been shown to bind to the catalytic (alpha) subunit of the Na+,K(+)-ATPase holoenzyme and the synthetic peptide sequence 496-HLLVMKGAPER-506, which includes Lys 501 (K), the major site for fluorescein-5'-isothiocyanate labeling of the Na+,K(+)-ATPase. This sequence region of alpha is proposed to comprise a portion of the enzyme's ATP binding domain (Taylor, W. R. & Green, N. W., 1989, Eur. J. Biochem. 179, 241-248). In this study we have determined M8-P1-A3's ability to recognize the alpha-subunit or homologous E1E2-ATPase proteins from different species and tissues in order to deduce the antibody's epitope. In addition the bacteriophage random peptide or 'epitope' library, recently developed by Scott and Smith (1990, Science 249, 386-390) and Devlin et al. (Devlin, J. J., Panganiban, L. C., & Devlin, P. E., 1990, Science 249, 404-406), has served as a convenient technique to confirm the species-specificity mapping data and to determine the exact amino acid requirements for antibody binding. The M8-P1-A3 epitope was found to consist of the five amino acid 494-PRHLL-498 sequence stretch of alpha, with residues PRxLx being critical for antibody recognition.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	12
Volume Number	2
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1993-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Triphosphate Metabolism Epitopes Immunology Peptide Fragments Sodium-potassium-exchanging Atpase Amino Acid Sequence Animals Binding Sites Inovirus Genetics Kidney Medulla Enzymology Molecular Sequence Data Rabbits Recombinant Proteins Species Specificity Surface Properties Swine Torpedo Xenopus Comparative Study Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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