Structure of the PIN/LC8 dimer with a bound peptide.
The structure of the protein known both as neuronal nitric oxide synthase inhibitory protein, PIN (protein inhibitor of nNOS), and also as the 8 kDa dynein light chain (LC8) has been solved by X-ray diffraction. Two PIN/LC8 monomers related by a two-fold axis form a rectangular dimer. Two pairs of alpha-helices cover opposite faces, and each pair of helices packs against a beta-sheet with five antiparallel beta-strands. Each five-stranded beta-sheet contains four strands from one monomer and a fifth strand from the other monomer. A 13-residue peptide from nNOS is bound to the dimer in a deep hydrophobic groove as a sixth antiparallel beta-strand. The structure provides key insights into dimerization of and peptide binding by the multifunctional PIN/LC8 protein.
Liang
J
J
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301, USA.
Jaffrey
S R
SR
Guo
W
W
Snyder
S H
SH
Clardy
J
J
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D019281:Dimerization; D029721:Drosophila Proteins; D004398:Dyneins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D019001:Nitric Oxide Synthase / Q000037:antagonists & inhibitors*; D052248:Nitric Oxide Synthase Type I; D011485:Protein Binding; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D002352:Carrier Proteins; D029721:Drosophila Proteins; D019001:Nitric Oxide Synthase; D052248:Nitric Oxide Synthase Type I; D004398:Dyneins