Proton nuclear magnetic resonance assignments and solution structure of a synthetic zinc finger from Xfin

A 25 residue synthetic peptide corresponding to zinc finger 31 of the Xenopus protein Xfin adopts a compact, folded conformation in the presence of zinc. Complete 1H resonance assignments have been made, and distance and dihedral angle constraints were used to generate structures using distance geom...

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Bibliographic Details
Published inStructure and methods : proceedings of the Sixth Conversation in the Discipline Biomolecular Stereodynamics held at the State University of New York at Albany, June 6-10, 1989 / edited by R.H. Sarma & M.H. Sarma pp. 83 - 91
Main Authors Lee, M.S, Gippert, G.P, Soman, K.V, Case, D.A, Wright, P.E
Format Publication
LanguageEnglish
Published Schenectady, NY : Adenine Press, c1990 1990
Subjects
binding sites
DNA
DNA-binding proteins
molecular conformation
nuclear magnetic resonance spectroscopy
synthetic peptides
Xenopus laevis
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Summary:A 25 residue synthetic peptide corresponding to zinc finger 31 of the Xenopus protein Xfin adopts a compact, folded conformation in the presence of zinc. Complete 1H resonance assignments have been made, and distance and dihedral angle constraints were used to generate structures using distance geometry and restrained molecular dynamics calculations. The polypeptide backbone fold consists of a well-defined helix, starting as alpha and ending as 3(10) helix, packed against two beta strands that are arranged in a hairpin structure. A high density of basic and polar amino acid side chains on the exposed face of the helix are probably involved in DNA binding.