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Structure of the PIN/LC8 dimer with a bound peptide

Nature Structural Biology volume 6, pages 735–740 (1999)Cite this article

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 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.

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Figure 1: The PIN/LC8 dimer complex.
Figure 2: Interactions between the bound peptide and PIN/LC8.
Figure 3: Sequences of PIN/LC8 and its homologs from various species are aligned by CLUSTALW29 and organized by Alscript30.
Figure 4: Gel-filtration behavior of PIN/LC8.

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Acknowledgements

The authors thank M.A. Iwamoto and T.K. Ly for help with PIN/LC8 crystallizations and S. Ealick and S. Liu for helpful discussions. This work was partially supported by USPHS grants (J.C., S.H.S., and S.R.J.) and a Research Scientist Award (S.H.S.).

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Authors and Affiliations

  1. Department of Chemistry and Chemical Biology, Cornell University, Ithaca, 14853-1301, New York, USA

    Jun Liang, Wei Guo & Jon Clardy

  2. Department of Neuroscience, Pharmacology and Molecular Sciences, and Psychiatry and Behavioral Sciences, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore , 21205, Maryland, USA

    Samie R. Jaffrey & Solomon H. Snyder

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Correspondence to Jon Clardy.

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Liang, J., Jaffrey, S., Guo, W. et al. Structure of the PIN/LC8 dimer with a bound peptide. Nat Struct Mol Biol 6, 735–740 (1999). https://doi.org/10.1038/11501

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