Pocketing the difference: structures of uracil excision repair proteins

Tom Ellenberger

doi:10.1016/1074-5521(95)90213-9

Pocketing the difference: structures of uracil excision repair proteins

Tom Ellenberger

Department of Biochemistry & Molecular Biophysics

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

7 Scopus citations

Abstract

The recognition of abnormal DNA structure by proteins is fundamentally different from sequence-specific DNA binding. Recent crystal structures of uracil-DNA glycosylases show a novel uracil-binding pocket that explains the enzyme's selectivity for uracil-containing DNA and provide a structural basis for exploring the catalytic mechanism of amino-glycosylic bond cleavage.

Original language	English
Pages (from-to)	351-354
Number of pages	4
Journal	Chemistry and Biology
Volume	2
Issue number	6
DOIs	https://doi.org/10.1016/1074-5521(95)90213-9
State	Published - Jun 1995

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10.1016/1074-5521(95)90213-9

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title = "Pocketing the difference: structures of uracil excision repair proteins",

abstract = "The recognition of abnormal DNA structure by proteins is fundamentally different from sequence-specific DNA binding. Recent crystal structures of uracil-DNA glycosylases show a novel uracil-binding pocket that explains the enzyme's selectivity for uracil-containing DNA and provide a structural basis for exploring the catalytic mechanism of amino-glycosylic bond cleavage.",

author = "Tom Ellenberger",

year = "1995",

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T2 - structures of uracil excision repair proteins

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N2 - The recognition of abnormal DNA structure by proteins is fundamentally different from sequence-specific DNA binding. Recent crystal structures of uracil-DNA glycosylases show a novel uracil-binding pocket that explains the enzyme's selectivity for uracil-containing DNA and provide a structural basis for exploring the catalytic mechanism of amino-glycosylic bond cleavage.

AB - The recognition of abnormal DNA structure by proteins is fundamentally different from sequence-specific DNA binding. Recent crystal structures of uracil-DNA glycosylases show a novel uracil-binding pocket that explains the enzyme's selectivity for uracil-containing DNA and provide a structural basis for exploring the catalytic mechanism of amino-glycosylic bond cleavage.

UR - https://www.scopus.com/pages/publications/0029310560

U2 - 10.1016/1074-5521(95)90213-9

DO - 10.1016/1074-5521(95)90213-9

M3 - Short survey

C2 - 9383436

AN - SCOPUS:0029310560

SN - 1074-5521

VL - 2

SP - 351

EP - 354

JO - Chemistry and Biology

JF - Chemistry and Biology

IS - 6

ER -

Pocketing the difference: structures of uracil excision repair proteins

Abstract

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