Sunghoon Kim's Aminoacyl-tRNA Synthetases in Biology and Medicine PDF


By Sunghoon Kim

ISBN-10: 940178700X

ISBN-13: 9789401787000

ISBN-10: 9401787018

ISBN-13: 9789401787017

This ebook will specialize in new molecular interactions and novel actions and the linked ailments which were lately came across from the experiences of eukaryotic and mammalian aminoacyl-tRNA synthetases. moreover, the capability purposes of ARS researches in biotechnology and medication could be addressed.

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Additional info for Aminoacyl-tRNA Synthetases in Biology and Medicine

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Schmitt E, Tanrikulu IC, Yoo TH, Panvert M, Tirrell DA, Mechulam Y (2009) Switching from an induced-fit to a lock-and-key mechanism in an aminoacyl-tRNA synthetase with modified specificity. J Mol Biol 394:843–851 72. Rath VL, Silvian LF, Beijer B, Sproat BS, Steitz TA (1998) How glutaminyl-tRNA synthetase selects glutamine. Structure 6:439–449 73. Bullock TL, Uter N, Nissan TA, Perona JJ (2003) Amino acid discrimination by a class I aminoacyl-tRNA synthetase specified by negative determinants.

In this case the editing active site plays a more active discriminatory role that includes specific conformational rearrangements [201]. Hydrogen bonds made by the threonine hydroxyl group to several conserved aspartates in the binding site also appear important to specificity [153]. The mechanisms of substrate specificity by class II aaRS are more idiosyncratic. ThrRS is able to exclude valine from the synthetic site based on a key role for a zinc ion in binding the side-chain hydroxyl group [112, 134].

However, such approaches must be employed cautiously because the extensive conformational changes of the protein, which occur concomitantly with translocation of the tRNA 30 -acceptor arm between the synthetic and editing domains, may readily generate pleiotropic effects for any mutation in either active site. The recent cocrystal structures of LeuRS bound to tRNA in both synthetic and editing conformations reveal that portions of the CP1 post-transfer editing domain extend directly into the synthetic active site [16].

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Aminoacyl-tRNA Synthetases in Biology and Medicine by Sunghoon Kim

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