Structure of the PIN/LC8 dimer with a bound peptide

J. Liang, S. R. Jaffrey, W. Guo, S. H. Snyder, J. Clardy

Research output: Contribution to journalArticlepeer-review

141 Scopus citations


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 α-helices cover opposite faces, and each pair of helices packs against a β-sheet with five antiparallel β-strands. Each five-stranded β- 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 β-strand. The structure provides key insights into dimerization of and peptide binding by the multifunctional PIN/LC8 protein.

Original languageEnglish (US)
Pages (from-to)735-740
Number of pages6
JournalNature Structural Biology
Issue number8
StatePublished - 1999
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics


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