Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta

Insights into the scaffold mechanism of human Rev1 in translesional synthesis revealed by structural studies on its polymerase-interacting domain

Protein interaction domain, UNP residues 1156-1251

peptide from DNA polymerase zeta catalytic subunit

Mitotic spindle assembly checkpoint protein MAD2B

Rev1, hRev1, Alpha integrin-binding protein 80, AIBP80, Rev1-like terminal deoxycytidyl transferase

Protein reversionless 3-like, REV3-like, hREV3

Mitotic arrest deficient 2-like protein 2, MAD2-like protein 2, REV7 homolog, hREV7

APNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDN
VQVVLQQTYGSTLKVT

TQDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVV
VILDKEHRPVEKFVFEITQPPLLSISSDSLLSHVEQLLRAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQV
IKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHK

0.1M HEPES-Na (pH 7.5), 0.1M NH4-citrate tribasic (pH 7.0), 19-21% PEG 3350, EVAPORATION, temperature 293K

Rev1, Rev3, Rev7, polymerase-interacting domain, Y-family polymerase, B-family polymerase, Translesional synthesis polymerase, DNA damage tolerance, Scaffold, TRANSFERASE-TRANSCRIPTION complex

QDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVV
ILDKEHRPVEKFVFEITQPPLLSISSDSLLSHVEQLLRAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVI
KDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHK