1a1u

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SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The p53 tumor suppressor oligomerization domain, a dimer of two primary, dimers, is an independently folding domain whose subunits consist of a, beta-strand, a tight turn and an alpha-helix. To evaluate the effect of, hydrophobic side-chains on three-dimensional structure, we substituted, residues Phe341 and Leu344 in the alpha-helix with other hydrophobic amino, acids. Substitutions that resulted in residue 341 having a smaller, side-chain than residue 344 switched the stoichiometry of the domain from, tetrameric to dimeric. The three-dimensional structure of one such dimer, was determined by multidimensional NMR spectroscopy. When compared with, the primary dimer of the wild-type p53 oligomerization domain, the mutant, dimer showed a switch in alpha-helical packing from anti-parallel to, parallel and rotation of the alpha-helices relative to the beta-strands., Hydrophobic side-chain size is therefore an important determinant of a, protein fold.

Disease

Known diseases associated with this structure: Adrenal cortical carcinoma OMIM:[191170], Breast cancer OMIM:[191170], Colorectal cancer OMIM:[191170], Hepatocellular carcinoma OMIM:[191170], Histiocytoma OMIM:[191170], Li-Fraumeni syndrome OMIM:[191170], Multiple malignancy syndrome OMIM:[191170], Nasopharyngeal carcinoma OMIM:[191170], Osteosarcoma OMIM:[191170], Pancreatic cancer OMIM:[191170], Thyroid carcinoma OMIM:[191170]

About this Structure

1A1U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain., McCoy M, Stavridi ES, Waterman JL, Wieczorek AM, Opella SJ, Halazonetis TD, EMBO J. 1997 Oct 15;16(20):6230-6. PMID:9321402

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