KA1 Domains: Unity in Mechanistic Diversity

Yi Ting Paung; Markus A. Seeliger

doi:10.1016/j.str.2018.07.002

KA1 Domains: Unity in Mechanistic Diversity

Yi Ting Paung
, Markus A. Seeliger

Pharmacological Sciences

Stony Brook University

Research output: Contribution to journal › Short survey › peer-review

4 Scopus citations

Abstract

The enzymatic activity of protein kinases is often tightly controlled by regulatory domains with a conserved structural mechanism. In this issue of Structure, Emptage et al. (2018) report how the kinase associated-1 domain (KA1) autoinhibits kinase activity with a striking structural diversity. The enzymatic activity of protein kinases is often tightly controlled by regulatory domains with a conserved structural mechanism. In this issue of Structure, Emptage et al. (2018) report how the kinase associated-1 domain (KA1) autoinhibits kinase activity with a striking structural diversity.

Original language	English
Pages (from-to)	1045-1047
Number of pages	3
Journal	Structure
Volume	26
Issue number	8
DOIs	https://doi.org/10.1016/j.str.2018.07.002
State	Published - Aug 7 2018

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title = "KA1 Domains: Unity in Mechanistic Diversity",

abstract = "The enzymatic activity of protein kinases is often tightly controlled by regulatory domains with a conserved structural mechanism. In this issue of Structure, Emptage et al. (2018) report how the kinase associated-1 domain (KA1) autoinhibits kinase activity with a striking structural diversity. The enzymatic activity of protein kinases is often tightly controlled by regulatory domains with a conserved structural mechanism. In this issue of Structure, Emptage et al. (2018) report how the kinase associated-1 domain (KA1) autoinhibits kinase activity with a striking structural diversity.",

author = "Paung, \{Yi Ting\} and Seeliger, \{Markus A.\}",

note = "Publisher Copyright: {\textcopyright} 2018 Elsevier Ltd",

year = "2018",

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AU - Seeliger, Markus A.

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N2 - The enzymatic activity of protein kinases is often tightly controlled by regulatory domains with a conserved structural mechanism. In this issue of Structure, Emptage et al. (2018) report how the kinase associated-1 domain (KA1) autoinhibits kinase activity with a striking structural diversity. The enzymatic activity of protein kinases is often tightly controlled by regulatory domains with a conserved structural mechanism. In this issue of Structure, Emptage et al. (2018) report how the kinase associated-1 domain (KA1) autoinhibits kinase activity with a striking structural diversity.

AB - The enzymatic activity of protein kinases is often tightly controlled by regulatory domains with a conserved structural mechanism. In this issue of Structure, Emptage et al. (2018) report how the kinase associated-1 domain (KA1) autoinhibits kinase activity with a striking structural diversity. The enzymatic activity of protein kinases is often tightly controlled by regulatory domains with a conserved structural mechanism. In this issue of Structure, Emptage et al. (2018) report how the kinase associated-1 domain (KA1) autoinhibits kinase activity with a striking structural diversity.

UR - https://www.scopus.com/pages/publications/85050693500

U2 - 10.1016/j.str.2018.07.002

DO - 10.1016/j.str.2018.07.002

M3 - Short survey

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AN - SCOPUS:85050693500

SN - 0969-2126

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SP - 1045

EP - 1047

JO - Structure

JF - Structure

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ER -

KA1 Domains: Unity in Mechanistic Diversity

Abstract

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