Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase γ, PolγB, functions as a homodimer

Molecular Cell

Volumn 7, Issue 1, 2001, Pages 43-54

  Carrodeguas, José A ^a   Theis, Karsten ^a,b   Bogenhagen, Daniel F ^a   Kisker, Caroline ^a,b  

^a STONY BROOK UNIVERSITY   (United States)

^b STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; DNA DIRECTED DNA POLYMERASE GAMMA; GLYCINE TRANSFER RNA LIGASE; HOLOENZYME; MUTANT PROTEIN;

ANALYTIC METHOD; ARTICLE; CRYSTAL STRUCTURE; DIMERIZATION; DNA BINDING; DNA HELIX; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME BINDING; ENZYME SUBUNIT; HUMAN; MAMMAL; MOUSE; NONHUMAN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; REACTION ANALYSIS; STRUCTURE ANALYSIS; XENOPUS LAEVIS;

MAMMALIA; XENOPUS LAEVIS;

EID: 0035101674     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(01)00153-8     Document Type: Article

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