1ILF

NMR STRUCTURE OF APO CBFB

1ILF の概要

• エントリーDOI: 10.2210/pdb1ilf/pdb
• 分子名称: CORE-BINDING FACTOR (1 entity in total)
• 機能のキーワード: partially open beta barrel, transcription
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Nucleus (Potential): Q08024
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16613.65

構造登録者

Wolf-Watz, M.,Grundstrom, T.,Hard, T. (登録日: 2001-05-08, 公開日: 2001-09-26, 最終更新日: 2024-05-22)

主引用文献

Wolf-Watz, M.,Grundstrom, T.,Hard, T.
Structure and backbone dynamics of Apo-CBFbeta in solution.
Biochemistry, 40:11423-11432, 2001

PubMed Abstract: Runx proteins constitute a family of mammalian transcription factors that interact with DNA through their evolutionarily conserved Runt domain. CBFbeta, alternatively denoted PEBP2beta, is the non-DNA-binding heterodimer partner and acts to enhance the DNA binding affinity of Runx proteins. Runx proteins and CBFbeta are associated with a variety of biological functions and human diseases; they are, for example, together the most frequent targets for chromosomal rearrangements in acute human leukemias. We have determined the solution structure and characterized the backbone dynamics of C-terminally truncated fragments containing residues 1-141 of CBFbeta. The present apo-CBFbeta structure is very similar to that seen in a Runt-CBFbeta complex. An evaluation of backbone (15)N NMR relaxation parameters shows that CBFbeta is a rigid molecule with high order parameters throughout the backbone; the only regions displaying significant dynamics are a long loop and the C-terminal alpha-helix. A few residues display relaxation behavior indicating conformational exchange on microsecond to millisecond time scales, but only one of these is located at the Runt binding surface. Our structure and dynamics analysis of CBFbeta therefore suggests that the protein binds to Runt without large conformational changes or induced folding ("lock-and-key" interaction). The apo-CBFbeta structure presented here exhibits several significant differences with two other published NMR ensembles of very similar protein fragments. The differences are located in four regions outside of the central beta-barrel, whereas the beta-barrel itself is almost identical in the three NMR structures. The comparison illustrates that independently determined NMR structures may display rather large differences in backbone conformation in regions that appear to be well-defined in each of the calculated NMR ensembles.

PubMed: 11560490
DOI: 10.1021/bi010713+

実験手法

SOLUTION NMR