Structure of the PIN/LC8 dimer with a bound peptide

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

doi:10.1038/11501

Structure of the PIN/LC8 dimer with a bound peptide

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

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141 Scopus citations

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.

Original language	English (US)
Pages (from-to)	735-740
Number of pages	6
Journal	Nature Structural Biology
Volume	6
Issue number	8
DOIs	https://doi.org/10.1038/11501
State	Published - 1999
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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10.1038/11501

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@article{a47a2234de954fdaa018900fcbab47a9,

title = "Structure of the PIN/LC8 dimer with a bound peptide",

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.",

author = "J. Liang and Jaffrey, {S. R.} and W. Guo and Snyder, {S. H.} and J. Clardy",

note = "Funding Information: 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.).",

year = "1999",

doi = "10.1038/11501",

language = "English (US)",

volume = "6",

pages = "735--740",

journal = "Nature Structural Biology",

issn = "1072-8368",

publisher = "Nature Publishing Group",

number = "8",

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TY - JOUR

T1 - Structure of the PIN/LC8 dimer with a bound peptide

AU - Liang, J.

AU - Jaffrey, S. R.

AU - Guo, W.

AU - Snyder, S. H.

AU - Clardy, J.

N1 - Funding Information: 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.).

PY - 1999

Y1 - 1999

N2 - 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.

AB - 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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JF - Nature Structural Biology

IS - 8

ER -

Structure of the PIN/LC8 dimer with a bound peptide

Abstract

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