Solution structure of the SH3 domain of phospholipase C-γ

D. Kohda; H. Hatanaka; M. Odaka; V. Mandiyan; A. Ullrich; J. Schlessinger; F. Inagaki

doi:10.1016/0092-8674(93)90583-C

Solution structure of the SH3 domain of phospholipase C-γ

D. Kohda, H. Hatanaka, M. Odaka, V. Mandiyan, A. Ullrich, J. Schlessinger, F. Inagaki

Research output: Contribution to journal › Article › peer-review

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Abstract

SH3 (Src homology 3) domains are found in many signaling proteins and appear to function as binding modules for cytoplasmic target proteins. The solution structure of the SH3 domain of human phospholipase C-γ (PLC-γ) was determined by two-dimensional ¹H NMR analysis. This SH3 domain is composed of eight antiparallel β strands consisting of two successive "Greek key" motifs, which form a barrel-like structure. The conserved aliphatic and aromatic residues form a hydrophobic pocket on the molecular surface, and the conserved carboxylic residues are localized to the periphery. The hydrophobic pocket may serve as a binding site for target proteins. Analysis of the slowly exchanging amide protons by NMR measurements indicates that despite containing a high content of β structure, the SH3 domain of PLC-γ is flexible.

Original language	English
Pages (from-to)	953-960
Number of pages	8
Journal	Cell
Volume	72
Issue number	6
DOIs	https://doi.org/10.1016/0092-8674(93)90583-C
Publication status	Published - Mar 26 1993
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry, Genetics and Molecular Biology(all)

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10.1016/0092-8674(93)90583-C

Cite this

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title = "Solution structure of the SH3 domain of phospholipase C-γ",

abstract = "SH3 (Src homology 3) domains are found in many signaling proteins and appear to function as binding modules for cytoplasmic target proteins. The solution structure of the SH3 domain of human phospholipase C-γ (PLC-γ) was determined by two-dimensional 1H NMR analysis. This SH3 domain is composed of eight antiparallel β strands consisting of two successive {"}Greek key{"} motifs, which form a barrel-like structure. The conserved aliphatic and aromatic residues form a hydrophobic pocket on the molecular surface, and the conserved carboxylic residues are localized to the periphery. The hydrophobic pocket may serve as a binding site for target proteins. Analysis of the slowly exchanging amide protons by NMR measurements indicates that despite containing a high content of β structure, the SH3 domain of PLC-γ is flexible.",

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T1 - Solution structure of the SH3 domain of phospholipase C-γ

AU - Kohda, D.

AU - Hatanaka, H.

AU - Odaka, M.

AU - Mandiyan, V.

AU - Ullrich, A.

AU - Schlessinger, J.

AU - Inagaki, F.

PY - 1993/3/26

Y1 - 1993/3/26

N2 - SH3 (Src homology 3) domains are found in many signaling proteins and appear to function as binding modules for cytoplasmic target proteins. The solution structure of the SH3 domain of human phospholipase C-γ (PLC-γ) was determined by two-dimensional 1H NMR analysis. This SH3 domain is composed of eight antiparallel β strands consisting of two successive "Greek key" motifs, which form a barrel-like structure. The conserved aliphatic and aromatic residues form a hydrophobic pocket on the molecular surface, and the conserved carboxylic residues are localized to the periphery. The hydrophobic pocket may serve as a binding site for target proteins. Analysis of the slowly exchanging amide protons by NMR measurements indicates that despite containing a high content of β structure, the SH3 domain of PLC-γ is flexible.

AB - SH3 (Src homology 3) domains are found in many signaling proteins and appear to function as binding modules for cytoplasmic target proteins. The solution structure of the SH3 domain of human phospholipase C-γ (PLC-γ) was determined by two-dimensional 1H NMR analysis. This SH3 domain is composed of eight antiparallel β strands consisting of two successive "Greek key" motifs, which form a barrel-like structure. The conserved aliphatic and aromatic residues form a hydrophobic pocket on the molecular surface, and the conserved carboxylic residues are localized to the periphery. The hydrophobic pocket may serve as a binding site for target proteins. Analysis of the slowly exchanging amide protons by NMR measurements indicates that despite containing a high content of β structure, the SH3 domain of PLC-γ is flexible.

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Solution structure of the SH3 domain of phospholipase C-γ

Abstract

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