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

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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.",

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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 - https://www.scopus.com/pages/publications/0035025570

M3 - Review article

AN - SCOPUS:0035025570

SN - 1431-9268

VL - 14

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EP - 147

JO - Chemtracts

JF - Chemtracts

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ER -

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

Abstract

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