Secondary structure of neutrophil-activating peptide-2 determined by 1H-nuclear magnetic resonance spectroscopy.
Neutrophil-activating protein-2 (NAP-2) is a 72 residue protein demonstrating a range of proinflammatory activities. The solution structure of monomeric NAP-2 has been investigated by two-dimensional 1H-n.m.r. spectroscopy. Sequence-specific proton resonance assignments have been made and secondary structural elements have been identified on the basis of nuclear Overhauser data, coupling constants and amide hydrogen/deuteron exchange. The NAP-2 monomer consists of a triple-stranded anti-parallel beta-sheet arranged in a 'Greek key' and a C-terminal helix (residues 59-70) and is very similar to that found in the n.m.r. solution conformation of dimeric interleukin-8 and the crystal structure of tetrameric bovine platelet factor-4. Results are discussed in terms of heparin binding and neutrophil-activation properties of NAP-2.
Mayo
K H
KH
Department of Biochemistry, University of Minnesota, Minneapolis 55455.
Yang
Y
Y
Daly
T J
TJ
Barry
J K
JK
La Rosa
G J
GJ
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D006801:Humans; D006863:Hydrogen-Ion Concentration; D016209:Interleukin-8 / Q000737:chemistry; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D010978:Platelet Factor 4 / Q000737:chemistry; D017433:Protein Structure, Secondary; D012996:Solutions; D001620:beta-Thromboglobulin
D016209:Interleukin-8; D046911:Macromolecular Substances; C061615:PPBP protein, human; D010455:Peptides; D012996:Solutions; D001620:beta-Thromboglobulin; D010978:Platelet Factor 4; C009862:connective tissue-activating peptide