Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy

David Fushman, Sean M. Cahill, Mark A. Lemmon, Joseph Schlessinger, David Cowburn

Research output: Contribution to journalArticle

81 Citations (Scopus)

Abstract

The pleckstrin homology (PH) domain is a recognition motif thought to be involved in signal-transduction pathways controlled by a variety of cytoplasmic proteins. Assignments of nearly all 1H, 13C, and 15N resonances of the PH domain from dynamin have been obtained from homonuclear and heteronuclear NMR experiments. The secondary structure has been elucidated from the pattern of nuclear Overhauser enhancements, from 13C chemical shift deviations, and from observation of slowly exchanging amide hydrogens. The secondary structure contains one α-helix and eight β- strands, seven of which are arranged in two contiguous, antiparallel β- sheets. The structure is monomeric, in contrast to the well-defined intimate dimerization of the crystal structure of this molecule. Residues possibly involved in ligand binding are in apparently flexible loops. Steady-state 15N{1H} nuclear Overhauser effect measurements indicate unequivocally the boundaries of this PH domain, and the structured portion of the domain appears to be more extended to the C terminus than previously suggested for other PH domains.

Original languageEnglish (US)
Pages (from-to)816-820
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number3
DOIs
StatePublished - Jan 31 1995
Externally publishedYes

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Biomolecular Nuclear Magnetic Resonance
Dynamins
Magnetic Resonance Spectroscopy
Dimerization
Amides
Hydrogen
Signal Transduction
Observation
Ligands
Pleckstrin Homology Domains
Proteins

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Solution structure of pleckstrin homology domain of dynamin by heteronuclear NMR spectroscopy. / Fushman, David; Cahill, Sean M.; Lemmon, Mark A.; Schlessinger, Joseph; Cowburn, David.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 92, No. 3, 31.01.1995, p. 816-820.

Research output: Contribution to journalArticle

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AU - Cowburn, David

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N2 - The pleckstrin homology (PH) domain is a recognition motif thought to be involved in signal-transduction pathways controlled by a variety of cytoplasmic proteins. Assignments of nearly all 1H, 13C, and 15N resonances of the PH domain from dynamin have been obtained from homonuclear and heteronuclear NMR experiments. The secondary structure has been elucidated from the pattern of nuclear Overhauser enhancements, from 13C chemical shift deviations, and from observation of slowly exchanging amide hydrogens. The secondary structure contains one α-helix and eight β- strands, seven of which are arranged in two contiguous, antiparallel β- sheets. The structure is monomeric, in contrast to the well-defined intimate dimerization of the crystal structure of this molecule. Residues possibly involved in ligand binding are in apparently flexible loops. Steady-state 15N{1H} nuclear Overhauser effect measurements indicate unequivocally the boundaries of this PH domain, and the structured portion of the domain appears to be more extended to the C terminus than previously suggested for other PH domains.

AB - The pleckstrin homology (PH) domain is a recognition motif thought to be involved in signal-transduction pathways controlled by a variety of cytoplasmic proteins. Assignments of nearly all 1H, 13C, and 15N resonances of the PH domain from dynamin have been obtained from homonuclear and heteronuclear NMR experiments. The secondary structure has been elucidated from the pattern of nuclear Overhauser enhancements, from 13C chemical shift deviations, and from observation of slowly exchanging amide hydrogens. The secondary structure contains one α-helix and eight β- strands, seven of which are arranged in two contiguous, antiparallel β- sheets. The structure is monomeric, in contrast to the well-defined intimate dimerization of the crystal structure of this molecule. Residues possibly involved in ligand binding are in apparently flexible loops. Steady-state 15N{1H} nuclear Overhauser effect measurements indicate unequivocally the boundaries of this PH domain, and the structured portion of the domain appears to be more extended to the C terminus than previously suggested for other PH domains.

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