Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/56262
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Type: | Journal article |
Title: | Crystallization and preliminary X-ray diffraction studies of the WW4 domain of the Nedd4-2 ubiquitin-protein ligase |
Author: | Umadevi, N. Kumar, S. Narayana, N. |
Citation: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2005; 61(PN Part 12):1084-1086 |
Publisher: | Blackwell Munksgaard |
Issue Date: | 2005 |
ISSN: | 1744-3091 1744-3091 |
Statement of Responsibility: | N. Umadevi, S. Kumar and N. Narayana |
Abstract: | Ubiquitin-mediated protein modification via covalent attachment of ubiquitin has emerged as one of the most common regulatory processes in all eukaryotes. Nedd4-2, closely related to neuronal precursor cell-expressed developmentally down-regulated 4 (Nedd4), is a multimodular ubiquitin-protein ligase comprised of four WW domains and a Hect domain. The WW domains recognize the proline-rich motifs on the multi-subunit amiloride-sensitive epithelial sodium channel (ENaC). To gain insights into the binding of the WW domain to proline-rich peptides, a protein fragment (78 amino acids) containing the fourth WW domain (WW4) of the Nedd4-2 protein was purified and crystallized and X-ray diffraction data were collected. A data set was obtained to 2.5 A resolution from a cryocooled single crystal at a synchrotron source. The crystals belong to the tetragonal space group P4(1)2(1)2 (or P4(3)2(1)2), with unit-cell parameters a = b = 113.43, c = 103.21 A. Analysis of the self-rotation function suggests the presence of four WW4 molecules in the asymmetric unit, with a high unit-cell solvent content of 74%. |
Keywords: | Nedd4-2 ubiquitin–protein ligase WW4 domain |
Description: | © 2005 International Union of Crystallography. All rights reserved. |
DOI: | 10.1107/S174430910503767X |
Description (link): | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1978143/ |
Published version: | http://dx.doi.org/10.1107/s174430910503767x |
Appears in Collections: | Aurora harvest 5 Medicine publications |
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