1olh

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HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The three-dimensional structure of the oligomerization domain (residues, 319 to 360) of the tumor suppressor p53 has been solved by, multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The, domain forms a 20-kilodalton symmetric tetramer with a topology made up, from a dimer of dimers. The two primary dimers each comprise two, antiparallel helices linked by an antiparallel beta sheet. One beta strand, and one helix are contributed from each monomer. The interface between the, two dimers forming the tetramer is mediated solely by helix-helix, contacts. The overall result is a symmetric, four-helix bundle with, adjacent helices oriented antiparallel to each other and with the two, antiparallel beta sheets located on opposing faces of the molecule. The, tetramer is stabilized not only by hydrophobic interactions within the, protein core but also by a number of electrostatic interactions. The, implications of the structure of the tetramer for the biological function, of p53 are discussed.

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

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

Reference

High-resolution structure of the oligomerization domain of p53 by multidimensional NMR., Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM, Science. 1994 Jul 15;265(5170):386-91. PMID:8023159

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