Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG

A. Y. Lau; M. D. Waytt; B. J. Glassner; L. D. Samson; T. Ellenberger; A. B. Guliaev; B. Singer

Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG

A. Y. Lau, M. D. Waytt, B. J. Glassner, L. D. Samson, T. Ellenberger, A. B. Guliaev, B. Singer

Department of Biochemistry & Molecular Biophysics

Research output: Contribution to journal › Review article › peer-review

Abstract

The crystal structure of the AAG/ A-DNA complex is extremely valuable in understanding the substrate specify and mechanism of excision repair by the human alkyladenine glycosylase. However, it is still different cult to obtain a complete picture of the entire functional pathway of the enzyme based solely on the crystal structure. Science should look forward to cocrystalization of the AAG enzyme complexed with other known substrates. This would be of great value in understanding the role of the adduct structure in the mechanism of mammalian DNA repair.

Original language	English
Pages (from-to)	142-147
Number of pages	6
Journal	Chemtracts
Volume	14
Issue number	3
State	Published - Jan 1 2001

Cite this

@article{b0b261ad7efb491ea12b655965e10bbd,

title = "Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG",

abstract = "The crystal structure of the AAG/ A-DNA complex is extremely valuable in understanding the substrate specify and mechanism of excision repair by the human alkyladenine glycosylase. However, it is still different cult to obtain a complete picture of the entire functional pathway of the enzyme based solely on the crystal structure. Science should look forward to cocrystalization of the AAG enzyme complexed with other known substrates. This would be of great value in understanding the role of the adduct structure in the mechanism of mammalian DNA repair.",

author = "Lau, {A. Y.} and Waytt, {M. D.} and Glassner, {B. J.} and Samson, {L. D.} and T. Ellenberger and Guliaev, {A. B.} and B. Singer",

year = "2001",

month = jan,

day = "1",

language = "English",

volume = "14",

pages = "142--147",

journal = "Chemtracts",

issn = "1431-9268",

number = "3",

}

TY - JOUR

T1 - Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG

AU - Lau, A. Y.

AU - Waytt, M. D.

AU - Glassner, B. J.

AU - Samson, L. D.

AU - Ellenberger, T.

AU - Guliaev, A. B.

AU - Singer, B.

PY - 2001/1/1

Y1 - 2001/1/1

N2 - The crystal structure of the AAG/ A-DNA complex is extremely valuable in understanding the substrate specify and mechanism of excision repair by the human alkyladenine glycosylase. However, it is still different cult to obtain a complete picture of the entire functional pathway of the enzyme based solely on the crystal structure. Science should look forward to cocrystalization of the AAG enzyme complexed with other known substrates. This would be of great value in understanding the role of the adduct structure in the mechanism of mammalian DNA repair.

AB - The crystal structure of the AAG/ A-DNA complex is extremely valuable in understanding the substrate specify and mechanism of excision repair by the human alkyladenine glycosylase. However, it is still different cult to obtain a complete picture of the entire functional pathway of the enzyme based solely on the crystal structure. Science should look forward to cocrystalization of the AAG enzyme complexed with other known substrates. This would be of great value in understanding the role of the adduct structure in the mechanism of mammalian DNA repair.

UR - http://www.scopus.com/inward/record.url?scp=0035025570&partnerID=8YFLogxK

M3 - Review article

AN - SCOPUS:0035025570

VL - 14

SP - 142

EP - 147

JO - Chemtracts

JF - Chemtracts

SN - 1431-9268

IS - 3

ER -

Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG

Abstract

Other files and links

Fingerprint

Cite this