Solution structure of a protein inhibitor of neuronal nitric oxide synthase

Nat Struct Biol. 1998 Nov;5(11):965-9. doi: 10.1038/2940.

Abstract

The structure of the neuronal nitric oxide synthase inhibitory protein, PIN (protein inhibitor of nNOS), has been determined by NMR spectroscopy. Two N-terminal antiparallel alpha-helices pack against a four-stranded antiparallel beta-sheet in the C-terminal region of the protein, forming a two-layer alpha/beta plait. The three dimensional structure of PIN resembles the fold of the B-chain of aspartylglucosaminidase. A non-prolyl cis peptide bond was found between Pro 52 and Thr 53 of the protein. PIN has a large solvent-exposed hydrophobic surface that contains a cavity and is rimmed with positive charges. This surface may serve as the primary target-binding region for this multi-functional regulatory protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Aspartylglucosylaminase / chemistry
  • Carrier Proteins / chemistry*
  • Crystallography, X-Ray
  • Drosophila Proteins*
  • Dyneins
  • Enzyme Inhibitors / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Nitric Oxide Synthase / antagonists & inhibitors*
  • Nitric Oxide Synthase Type I
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Structure, Secondary
  • Rats

Substances

  • Carrier Proteins
  • Drosophila Proteins
  • Enzyme Inhibitors
  • Nitric Oxide Synthase
  • Nitric Oxide Synthase Type I
  • Nos1 protein, rat
  • Aspartylglucosylaminase
  • Dyneins

Associated data

  • PDB/1BKQ
  • PDB/R1BKQMR