Solution structure of the SH3 domain of phospholipase C-γ

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

Research output: Contribution to journalArticle

99 Citations (Scopus)

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 languageEnglish
Pages (from-to)953-960
Number of pages8
JournalCell
Volume72
Issue number6
DOIs
Publication statusPublished - Mar 26 1993

Fingerprint

src Homology Domains
Type C Phospholipases
Nuclear magnetic resonance
Proteins
Amides
Protons
Binding Sites

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Kohda, D., Hatanaka, H., Odaka, M., Mandiyan, V., Ullrich, A., Schlessinger, J., & Inagaki, F. (1993). Solution structure of the SH3 domain of phospholipase C-γ. Cell, 72(6), 953-960. https://doi.org/10.1016/0092-8674(93)90583-C

Solution structure of the SH3 domain of phospholipase C-γ. / Kohda, Daisuke; Hatanaka, H.; Odaka, M.; Mandiyan, V.; Ullrich, A.; Schlessinger, J.; Inagaki, F.

In: Cell, Vol. 72, No. 6, 26.03.1993, p. 953-960.

Research output: Contribution to journalArticle

Kohda, D, Hatanaka, H, Odaka, M, Mandiyan, V, Ullrich, A, Schlessinger, J & Inagaki, F 1993, 'Solution structure of the SH3 domain of phospholipase C-γ', Cell, vol. 72, no. 6, pp. 953-960. https://doi.org/10.1016/0092-8674(93)90583-C
Kohda D, Hatanaka H, Odaka M, Mandiyan V, Ullrich A, Schlessinger J et al. Solution structure of the SH3 domain of phospholipase C-γ. Cell. 1993 Mar 26;72(6):953-960. https://doi.org/10.1016/0092-8674(93)90583-C
Kohda, Daisuke ; Hatanaka, H. ; Odaka, M. ; Mandiyan, V. ; Ullrich, A. ; Schlessinger, J. ; Inagaki, F. / Solution structure of the SH3 domain of phospholipase C-γ. In: Cell. 1993 ; Vol. 72, No. 6. pp. 953-960.
@article{ae6467358ebb477a8e58e1121aad3687,
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.",
author = "Daisuke Kohda and H. Hatanaka and M. Odaka and V. Mandiyan and A. Ullrich and J. Schlessinger and F. Inagaki",
year = "1993",
month = "3",
day = "26",
doi = "10.1016/0092-8674(93)90583-C",
language = "English",
volume = "72",
pages = "953--960",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "6",

}

TY - JOUR

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

AU - Kohda, Daisuke

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.

UR - http://www.scopus.com/inward/record.url?scp=0027537997&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027537997&partnerID=8YFLogxK

U2 - 10.1016/0092-8674(93)90583-C

DO - 10.1016/0092-8674(93)90583-C

M3 - Article

C2 - 7681365

AN - SCOPUS:0027537997

VL - 72

SP - 953

EP - 960

JO - Cell

JF - Cell

SN - 0092-8674

IS - 6

ER -