The structure of the amino terminal transforming segment of the p21 protein, Tyr4-Thr20 (with Asp12), by two-dimensional NMR

P. A. Longo; M. S. Broido; J. Chen; H. F. Kung; M. R. Pincus

doi:10.1016/S0006-291X(88)80317-6

The structure of the amino terminal transforming segment of the p21 protein, Tyr⁴-Thr²⁰ (with Asp¹²), by two-dimensional NMR

P. A. Longo, M. S. Broido, J. Chen, H. F. Kung, M. R. Pincus

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

2 Scopus citations

Abstract

The structure of a peptide from the transforming region (residues 4 - 20) of the p21 protein has been determined using two-dimensional NMR. In the normal protein, this segment contains a Gly residue at the critical 12 position; any substitution, other than Pro, at this position results in a transforming protein. Previously performed energy calculations indicated that this peptide segment is a structured one. In this study we find that the Asp¹² containing peptide has a surprisingly well-defined structure in solution which has more similarity to the GDP-binding loop region in EF-tu than to that in p21.

Original language	English
Pages (from-to)	776-782
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	157
Issue number	2
DOIs	https://doi.org/10.1016/S0006-291X(88)80317-6
State	Published - 15 Dec 1988
Externally published	Yes

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@article{c37fb1805d6e4b9dbcaec88cfe7961fc,

title = "The structure of the amino terminal transforming segment of the p21 protein, Tyr4-Thr20 (with Asp12), by two-dimensional NMR",

abstract = "The structure of a peptide from the transforming region (residues 4 - 20) of the p21 protein has been determined using two-dimensional NMR. In the normal protein, this segment contains a Gly residue at the critical 12 position; any substitution, other than Pro, at this position results in a transforming protein. Previously performed energy calculations indicated that this peptide segment is a structured one. In this study we find that the Asp12 containing peptide has a surprisingly well-defined structure in solution which has more similarity to the GDP-binding loop region in EF-tu than to that in p21.",

author = "Longo, {P. A.} and Broido, {M. S.} and J. Chen and Kung, {H. F.} and Pincus, {M. R.}",

note = "Funding Information: Acknowledgements: The authors gratefully acknowledge support for this project from NIH (CA 42500, to MRP) and a {"}Research Centers in Minority Institutions{"} award (RR-03037 from DRR, NIH) to Hunter College (MSB). NSF grant PCM8111745 in support of the CUNY NMR spectrometer is gratefully acknowledged. The New York University ACF Computing Center has provided strong support of the computing aspects of this study.",

year = "1988",

month = dec,

day = "15",

doi = "10.1016/S0006-291X(88)80317-6",

language = "English",

volume = "157",

pages = "776--782",

journal = "Biochemical and Biophysical Research Communications",

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publisher = "Academic Press Inc.",

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TY - JOUR

T1 - The structure of the amino terminal transforming segment of the p21 protein, Tyr4-Thr20 (with Asp12), by two-dimensional NMR

AU - Longo, P. A.

AU - Broido, M. S.

AU - Chen, J.

AU - Kung, H. F.

AU - Pincus, M. R.

N1 - Funding Information: Acknowledgements: The authors gratefully acknowledge support for this project from NIH (CA 42500, to MRP) and a "Research Centers in Minority Institutions" award (RR-03037 from DRR, NIH) to Hunter College (MSB). NSF grant PCM8111745 in support of the CUNY NMR spectrometer is gratefully acknowledged. The New York University ACF Computing Center has provided strong support of the computing aspects of this study.

PY - 1988/12/15

Y1 - 1988/12/15

N2 - The structure of a peptide from the transforming region (residues 4 - 20) of the p21 protein has been determined using two-dimensional NMR. In the normal protein, this segment contains a Gly residue at the critical 12 position; any substitution, other than Pro, at this position results in a transforming protein. Previously performed energy calculations indicated that this peptide segment is a structured one. In this study we find that the Asp12 containing peptide has a surprisingly well-defined structure in solution which has more similarity to the GDP-binding loop region in EF-tu than to that in p21.

AB - The structure of a peptide from the transforming region (residues 4 - 20) of the p21 protein has been determined using two-dimensional NMR. In the normal protein, this segment contains a Gly residue at the critical 12 position; any substitution, other than Pro, at this position results in a transforming protein. Previously performed energy calculations indicated that this peptide segment is a structured one. In this study we find that the Asp12 containing peptide has a surprisingly well-defined structure in solution which has more similarity to the GDP-binding loop region in EF-tu than to that in p21.

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U2 - 10.1016/S0006-291X(88)80317-6

DO - 10.1016/S0006-291X(88)80317-6

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AN - SCOPUS:0024264783

SN - 0006-291X

VL - 157

SP - 776

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

The structure of the amino terminal transforming segment of the p21 protein, Tyr4-Thr20 (with Asp12), by two-dimensional NMR

Abstract

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The structure of the amino terminal transforming segment of the p21 protein, Tyr⁴-Thr²⁰ (with Asp¹²), by two-dimensional NMR