Kodai Hara, Toshiyuki Shimizu, Satoru Unzai, Satoko Akashi, Mamoru Sato, Hiroshi Hashimoto
Graduate School of Nanobioscience, Yokohama City University, 1-7-29 Suehiro, Tsurumi, Yokohama, Kanagawa 230-0045, Japan.
Acta crystallographica. Section F, Structural biology and crystallization communications 2009 Dec 1REV7 is involved in various cellular functions including DNA replication, signal transduction and cell-cycle regulation. In DNA replication, REV7 interacts with REV3 and forms DNA polymerase zeta, which plays a central role in error-prone DNA synthesis. REV3 is a catalytic subunit and its activity is stimulated by REV7. To clarify the structural basis of the interaction between REV7 and REV3, human REV7 was crystallized in complex with a REV3 fragment. Two crystal forms were obtained. Crystal forms I and II belonged to space groups P2(1), with unit-cell parameters a = 43.8, b = 50.0, c = 107.3 A, beta = 96.9 degrees , and P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 76.6, c = 118.4 A, respectively.
Kodai Hara, Toshiyuki Shimizu, Satoru Unzai, Satoko Akashi, Mamoru Sato, Hiroshi Hashimoto. Purification, crystallization and initial X-ray diffraction study of human REV7 in complex with a REV3 fragment. Acta crystallographica. Section F, Structural biology and crystallization communications. 2009 Dec 1;65(Pt 12):1302-5
PMID: 20054135
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