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The crystal structure of the ubiquitin-like (UbL) domain of human homologue A of Rad23 (hHR23A) protein

DOI: 10.1093/protein/gzq084 DOI Help
PMID: 21047872 PMID Help

Authors: Y. W. Chen (King's College London) , T. Tajima (King's College London) , S. Agrawal (King's College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Protein Engineering Design And Selection , VOL 24 , PAGES 131 - 138

State: Published (Approved)
Published: December 2010
Diamond Proposal Number(s): 1220

Abstract: The human homologue of the yeast Rad23 protein, hHR23A, plays dual roles in DNA repair as well as in translocating polyubiquitinated proteins to the proteasome. We determined the three-dimensional structure of its ubiquitin-like (UbL) domain by X-ray crystallography. It has the same overall structure and fold characteristics as ubiquitin and other members of the UbL domain family, with overall root mean square deviations in C? positions in the range of 1.0–1.3 Å. There are local differences in the ?1–?3 loop where hHR23A UbL domain has three more residues constituting a bigger loop. Analysis of the crystal packing revealed a possible dimeric arrangement mediated by the three residues (Leu10, Ile49 and Met75) that are known to be critical for molecular interactions. In contrast to the overall well-defined structure, these three residues are either disordered or have multiple conformations, suggesting that conformation variability is an important property of the binding surface. The electrostatic potentials at the binding surface are conserved among the family, with the hHR23B domain being the most similar to this structure. The intra-molecular complexes formed by the UbL domain of hHR23A with its UbA1 or UbA2 domains was studied by comparative homology modelling, which suggests these two interactions are structurally similar and are mutually exclusive.

Journal Keywords: X-Ray; DNA; DNA-Binding; Humans; Models; Molecular; Protein; Tertiary; Ubiquitin

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

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