Is acetylation the key to opening locked gates?

B. Franklin Pugh

doi:10.1038/nsmb0404-298

Is acetylation the key to opening locked gates?

B. Franklin Pugh

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

2 Scopus citations

Abstract

Like certain protein kinases, some protein acetyltransferases such as p300 may use an inhibitory loop that can be regulated to limit the accessibility of substrates to its active site. The finding that autoacetylation of this loop activates the acetyltransferase provides the first evidence for an acetylation cascade analogous to protein kinase cascades.

Original language	English (US)
Pages (from-to)	298-300
Number of pages	3
Journal	Nature Structural and Molecular Biology
Volume	11
Issue number	4
DOIs	https://doi.org/10.1038/nsmb0404-298
State	Published - Apr 2004

All Science Journal Classification (ASJC) codes

Structural Biology
Molecular Biology

Access to Document

10.1038/nsmb0404-298

Cite this

@article{2c81b3ec89634229b13fe0aff68fc8f7,

title = "Is acetylation the key to opening locked gates?",

abstract = "Like certain protein kinases, some protein acetyltransferases such as p300 may use an inhibitory loop that can be regulated to limit the accessibility of substrates to its active site. The finding that autoacetylation of this loop activates the acetyltransferase provides the first evidence for an acetylation cascade analogous to protein kinase cascades.",

author = "Pugh, {B. Franklin}",

year = "2004",

month = apr,

doi = "10.1038/nsmb0404-298",

language = "English (US)",

volume = "11",

pages = "298--300",

journal = "Nature Structural and Molecular Biology",

issn = "1545-9993",