Structure of the PIN/LC8 dimer with a bound peptide

Nat Struct Biol. 1999 Aug;6(8):735-40. doi: 10.1038/11501.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Carrier Proteins / chemistry*
  • Crystallography, X-Ray
  • Dimerization
  • Drosophila Proteins*
  • Dyneins / chemistry*
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Nitric Oxide Synthase / antagonists & inhibitors*
  • Nitric Oxide Synthase Type I
  • Protein Binding
  • Protein Conformation
  • Sequence Homology, Amino Acid

Substances

  • Carrier Proteins
  • Drosophila Proteins
  • Nitric Oxide Synthase
  • Nitric Oxide Synthase Type I
  • Dyneins

Associated data

  • PDB/1CMI