1c26

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Revision as of 14:10, 12 November 2007

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spinqualitylabelsall models 1c26, resolution 1.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF P53 TETRAMERIZATION DOMAIN

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The p53 protein is a tetrameric transcription factor that plays a central, role in the prevention of neoplastic transformation. Oligomerization, appears to be essential for the tumor suppressing activity of p53 because, oligomerization-deficient p53 mutants cannot suppress the growth of, carcinoma cell lines. The crystal structure of the tetramerization domain, of p53 (residues 325 to 356) was determined at 1.7 angstrom resolution and, refined to a crystallographic R factor of 19.2 percent. The monomer, which, consists of a beta strand and an alpha helix, associates with a second, monomer across an antiparallel beta sheet and an antiparallel helix-helix, interface to form a dimer. Two of these dimers associate across a second, and distinct parallel helix-helix interface to form the tetramer.

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

1C26 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms., Jeffrey PD, Gorina S, Pavletich NP, Science. 1995 Mar 10;267(5203):1498-502. PMID:7878469

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