Crystallization and preliminary studies of the DNA-binding runt domain of AML1

被引：4

作者：

Bäckström, S

Huang, SH

Wolf-Watz, M

Xie, XQ

Härd, T

Grundström, T

Sauer, UH ^{[1
]}

机构：

[1] Umea Univ, UCMP, SE-90187 Umea, Sweden

[2] Royal Inst Technol, Dept Biotechnol, SE-14157 Huddinge, Sweden

[3] Univ Ottawa, Fac Med, CMM, Ottawa, ON K1G 8M5, Canada

[4] Umea Univ, Dept Cell & Mol Biol, Div Tumour Biol, SE-90187 Umea, Sweden

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2001年 / 57卷

关键词：

D O I：

10.1107/S0907444900015791

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The acute myeloid leukaemia 1 (AML1) protein belongs to the Runx family of transcription factors and is crucial for haematopoietic development. The genes encoding Runx1 and its associated factor CBF beta are the most frequent targets for chromosomal rearrangements in acute human leukaemias. In addition, point mutations of Runx1 in acute leukaemias and in the familial platelet disorder FPD/AML cluster within the evolutionary conserved runt domain that binds both DNA and CBF beta. Here, the crystallization of the Runx1 runt domain is reported. Crystals belong to space groups C2 and R32 and diffract to 1.7 and 2.0 Angstrom resolution, respectively.

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页码：269 / 271

页数：3

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