Structural highlights
Publication Abstract from PubMed
The structure of onconase C30A/C75A double mutant has been determined at 1.12A resolution. The structure has high structural homology to other onconase structures. The changes being results of mutation are relatively small, distributed asymmetrically around the two mutated positions, and they are observed not only in the mutation region but expanded to entire molecule. Different conformation of Lys31 side chain that influences the hydrogen bonding network around catalytic triad is probably responsible for lower catalytic efficiency of double mutant. The decrease in thermal stability observed for the onconase variant might be explained by a less dense packing as manifested by the increase of the molecular volume and the solvent accessible surface area. (c) 2013 Wiley Periodicals, Inc. Biopolymers 101: 454-460, 2014.
Investigating the effects of double mutation C30A/C75A on onconase structure: Studies at atomic resolution.,Kurpiewska K, Torrent G, Ribo M, Loch JI, Vilanova M, Lewinski K Biopolymers. 2014 May;101(5):454-60. doi: 10.1002/bip.22403. PMID:23996687[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kurpiewska K, Torrent G, Ribo M, Loch JI, Vilanova M, Lewinski K. Investigating the effects of double mutation C30A/C75A on onconase structure: Studies at atomic resolution. Biopolymers. 2014 May;101(5):454-60. doi: 10.1002/bip.22403. PMID:23996687 doi:http://dx.doi.org/10.1002/bip.22403
