3T1I

Crystal Structure of Human Mre11: Understanding Tumorigenic Mutations

3T1I の概要

• エントリーDOI: 10.2210/pdb3t1i/pdb
• 分子名称: Double-strand break repair protein MRE11A, MANGANESE (II) ION, 2,3-DIHYDROXY-1,4-DITHIOBUTANE, ... (5 entities in total)
• 機能のキーワード: dna repair, mrn complex, metallophosphatase, exonuclease, endonuclease, rad50, nbs1, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus (By similarity): P49959
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 201428.71

構造登録者

Park, Y.B.,Chae, J.,Kim, Y.,Cho, Y. (登録日: 2011-07-22, 公開日: 2011-11-30, 最終更新日: 2024-11-20)

主引用文献

Park, Y.B.,Chae, J.,Kim, Y.,Cho, Y.
Crystal structure of human mre11: understanding tumorigenic mutations
Structure, 19:1591-1602, 2011

PubMed Abstract: Mre11 plays an important role in repairing damaged DNA by cleaving broken ends and by providing a platform for other DNA repair proteins. Various Mre11 mutations have been identified in several types of cancer. We have determined the crystal structure of the human Mre11 core (hMre11), which contains the nuclease and capping domains. hMre11 dimerizes through the interfaces between loop β3-α3 from one Mre11 and loop β4-β5 from another Mre11, and between loop α2-β3 from one Mre11 and helices α2 and α3 from another Mre11, and assembles into a completely different dimeric architecture compared with bacterial or archaeal Mre11 homologs. Nbs1 binds to the region containing loop α2-β3 which participates in dimerization. The hMre11 structure in conjunction with biochemical analyses reveals that many tumorigenic mutations are primarily associated with Nbs1 binding and partly with nuclease activities, providing a framework for understanding how mutations inactivate Mre11.

PubMed: 22078559
DOI: 10.1016/j.str.2011.09.010

実験手法

X-RAY DIFFRACTION (3 Å)