1aar

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(New page: 200px<br /><applet load="1aar" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aar, resolution 2.3&Aring;" /> '''STRUCTURE OF A DIUBIQ...)
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Revision as of 08:36, 20 November 2007


1aar, resolution 2.3Å

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STRUCTURE OF A DIUBIQUITIN CONJUGATE AND A MODEL FOR INTERACTION WITH UBIQUITIN CONJUGATING ENZYME (E2)

Overview

Covalent ligation of multiubiquitin chains targets eukaryotic proteins for, degradation. In such multiubiquitin chains, successive ubiquitins are, linked by an isopeptide bond involving the side chain of Lys48 and the, carboxyl group of Gly76. The crystal structure of a diubiquitin conjugate, has been determined and refined at 2.3-A resolution. The molecule has, internal approximate 2-fold symmetry with multiple hydrophobic and, hydrophilic contacts along the 2-fold axis. The structure of the, diubiquitin conjugate suggests determinants for recognition of, multiubiquitin chains. A model for the interaction of diubiquitin and a, ubiquitin conjugating enzyme (E2) is proposed.

About this Structure

1AAR is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2)., Cook WJ, Jeffrey LC, Carson M, Chen Z, Pickart CM, J Biol Chem. 1992 Aug 15;267(23):16467-71. PMID:1322903

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