Protein kinases

Elizabeth J. Goldsmith; Melanie H. Cobb

doi:10.1016/0959-440X(94)90264-X

Protein kinases

Elizabeth J. Goldsmith, Melanie H. Cobb

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

65 Scopus citations

Abstract

The structures of four serine/threonine protein kinases have been determined recently. By comparing these structures with that of the cAMP-dependent protein kinase (cAPK), it is now possible to see how the activity of these regulatory enzymes is controlled. Low activity is maintained through the conformation of the phosphorylation lip, domain rotations, and binding of substrate analog inhibitors and autoinhibitory domains.

Original language	English (US)
Pages (from-to)	833-840
Number of pages	8
Journal	Current Opinion in Structural Biology
Volume	4
Issue number	6
DOIs	https://doi.org/10.1016/0959-440X(94)90264-X
State	Published - 1994

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/0959-440X(94)90264-X

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title = "Protein kinases",

abstract = "The structures of four serine/threonine protein kinases have been determined recently. By comparing these structures with that of the cAMP-dependent protein kinase (cAPK), it is now possible to see how the activity of these regulatory enzymes is controlled. Low activity is maintained through the conformation of the phosphorylation lip, domain rotations, and binding of substrate analog inhibitors and autoinhibitory domains.",

author = "Goldsmith, {Elizabeth J.} and Cobb, {Melanie H.}",

year = "1994",

doi = "10.1016/0959-440X(94)90264-X",

language = "English (US)",

volume = "4",

pages = "833--840",

journal = "Current Opinion in Structural Biology",

issn = "0959-440X",

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AU - Goldsmith, Elizabeth J.

AU - Cobb, Melanie H.

PY - 1994

Y1 - 1994

N2 - The structures of four serine/threonine protein kinases have been determined recently. By comparing these structures with that of the cAMP-dependent protein kinase (cAPK), it is now possible to see how the activity of these regulatory enzymes is controlled. Low activity is maintained through the conformation of the phosphorylation lip, domain rotations, and binding of substrate analog inhibitors and autoinhibitory domains.

AB - The structures of four serine/threonine protein kinases have been determined recently. By comparing these structures with that of the cAMP-dependent protein kinase (cAPK), it is now possible to see how the activity of these regulatory enzymes is controlled. Low activity is maintained through the conformation of the phosphorylation lip, domain rotations, and binding of substrate analog inhibitors and autoinhibitory domains.

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U2 - 10.1016/0959-440X(94)90264-X

DO - 10.1016/0959-440X(94)90264-X

M3 - Article

C2 - 7712287

AN - SCOPUS:0028557025

SN - 0959-440X

VL - 4

SP - 833

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JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

IS - 6

ER -

Protein kinases

Abstract

ASJC Scopus subject areas

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