The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites.

Gorman, M A; Morera, S; Rothwell, D G; de La Fortelle, E; Mol, C D; Tainer, J A; Hickson, I D; Freemont, P S

Gorman, M A; Morera, S; Rothwell, D G; de La Fortelle, E; Mol, C D; Tainer, J A; Hickson, I D; Freemont, P S.

Affiliation

Gorman MA; Protein Structure Laboratory, Imperial Cancer Research Fund, London, UK.

EMBO J ; 16(21): 6548-58, 1997 Nov 03.

Article in En | MEDLINE | ID: mdl-9351835

Subject(s)

Carbon-Oxygen Lyases; DNA-(Apurinic or Apyrimidinic Site) Lyase; Endonucleases/chemistry; Nuclear Proteins/chemistry; Protein Conformation; Amino Acid Sequence; Animals; Bacterial Proteins/chemistry; Binding Sites; Cattle; Crystallography, X-Ray; DNA/metabolism; DNA Repair; Deoxyribonuclease I/chemistry; Escherichia coli/chemistry; Exodeoxyribonucleases/chemistry; Humans; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Protein Binding; Recombinant Fusion Proteins/chemistry; Sequence Alignment; Sequence Homology, Amino Acid

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Protein Conformation / Nuclear Proteins / Carbon-Oxygen Lyases / DNA-(Apurinic or Apyrimidinic Site) Lyase / Endonucleases Limits: Animals / Humans Language: En Journal: EMBO J Year: 1997 Document type: Article Affiliation country: United kingdom Country of publication: United kingdom

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