Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2013 Apr 23;81(10):1840–1846. doi: 10.1002/prot.24306

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2013 Wiley Periodicals, Inc.

Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.

PMC Copyright notice

N-terminal extension, PTM, and key intermolecular interaction of DRS. (A) The switching model of the N-helix with our DRS structure. (B) PTM analyses. Acetylation, phosphorylation, and ubiquitination sites are shown as blue, red, and yellow circles, respectively. PTM sites uniquely observed in this study and residues observed both in the database and in our study are surrounded by black boxes and dotted boxes, respectively. Ser146, which is expected to play a key role in the organization of DRS, is marked with a red asterisk. (C) Sequence alignment of the interface residues of anticodon-binding domain and catalytic domain of DRSs from various organisms. Ser146, Gly462, and Ala463 of human DRS are marked with red asterisks. (D) Close-up view of Ser146 and the intermolecular interaction of DRS dimer. The structure of human DRS is superimposed with that of human KRS shown in a gray cartoon model.