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Proton NMR assignments and secondary structure of the snake venom protein echistatin

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00114a004· OSTI ID:5617495
;  [1]; ; ; ;  [2]
  1. Rutgers-the State Univ., Piscataway, NJ (United States)
  2. Merck Sharp and Dohme Research Labs., West Point, PA (United States)
The snake venom protein echistatin is a potent inhibitor of platelet aggregation. The inhibitory properties of echistatin have been attributed to the Arg-Gly-Asp sequence at residues 24-26. In this paper, sequence-specific nuclear magnetic resonance assignments are presented for the proton resonances of echistatin in water. The single-chain protein contains 49 amino acids and 4 cystine bridges. All of the backbone amide, C{sub alpha}H, and side-chain resonances, except for the {eta}-NH of the arginines, have been assigned. The secondary structure of the protein was characterized from the pattern of nuclear Overhauser enhancements, from the identification of slowly exchanging amide protons, from {sup 3}J{sub c{alpha}H-NH} coupling constants, and from circular dichroism studies. The data suggest that the secondary structure consists of a type I {beta}-turn, a short {beta}-hairpin, and a short-, irregular, antiparallel {beta}-sheet and that the Arg-Gly-Asp sequence is in a flexible loop connecting two strands of the distorted antiparallel {beta}-sheet.
OSTI ID:
5617495
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 30:50; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English