2oeh

From Proteopedia

Revision as of 12:16, 23 January 2008

Determination of the Three-dimensional Structure of the Mrf2-DNA Complex Using Paramagnetic Spin Labeling

Overview

Understanding the mechanism of protein-DNA interactions at the molecular, level is one of the main focuses in structural and molecular biological, investigations. At present, NMR spectroscopy is the only approach that can, provide atomic details of protein-DNA recognition in solution. However, determining the structures of protein-DNA complexes using NMR spectroscopy, has been dependent on the observation of intermolecular nuclear Overhauser, effects (NOE) and their assignments, which are difficult to obtain in many, cases. In this study, we have shown that intermolecular distance, constraints derived from a single spin-label in combination with docking, calculations have defined many specific contacts of the complex between, the AT-rich interaction domain (ARID) of Mrf2 and its target DNA. Mrf2, contacts DNA mainly using the two flexible loops, L1 and L2. While the L1, loop contacts the phosphate backbone, L2 and several residues in the, adjacent helices interact with AT base pairs in the major groove of DNA., Despite the structural diversity in the ARID family of DNA-binding, proteins, Mrf2 maintains contacts with DNA similar to those observed in, the homologous Dri-DNA complex.

About this Structure

2OEH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Determination of the three-dimensional structure of the Mrf2-DNA complex using paramagnetic spin labeling., Cai S, Zhu L, Zhang Z, Chen Y, Biochemistry. 2007 May 1;46(17):4943-50. Epub 2007 Apr 4. PMID:17407261

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