Insights into nonspecific binding of homeodomains from a structure of MATα2 bound to DNA

被引：13

作者：

Aishima, J

Wolberger, C

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Biophys & Biophys Chem, Baltimore, MD 21205 USA

[2] Howard Hughes Med Inst, Baltimore, MD USA

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2003年 / 51卷 / 04期

关键词：

DNA-binding protein; homeodomain; nonspecific binding; X-ray crystallography;

D O I：

10.1002/prot.10375

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The 2.1-Angstrom resolution crystal structure of the MATalpha2 homeodomain bound to DNA reveals the unexpected presence of two nonspecifically bound alpha2 homeodomains, in addition to the two alpha2 homeodomains bound to canonical alpha2 binding sites. One of the extra homeodomains makes few base-specific contacts, while the other extra homeodomain binds to DNA in a previously unobserved manner. This unusually bound homeodomain is rotated on the DNA, making possible major groove contacts by side-chains that normally do not contact the DNA. This alternate docking may represent one way in which homeodomains sample nonspecific DNA sequences.

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收藏

页码：544 / 551

页数：8

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