BMB Reports
- Volume 51 Issue 12
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- Pages.609-610
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- 2018
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- 1976-670X(eISSN)
DOI QR Code
Structural insights showing how arginine is able to be glycosylated by pathogenic effector proteins
- Park, Jun Bae (Department of Systems Biology and College of Life Science and Biotechnology, Yonsei University) ;
- Yoo, Youngki (Department of Systems Biology and College of Life Science and Biotechnology, Yonsei University) ;
- Cho, Hyun-Soo (Department of Systems Biology and College of Life Science and Biotechnology, Yonsei University)
- Received : 2018.11.07
- Published : 2018.12.31
Abstract
Glycosylation is one form of protein modification and plays a key role in protein stability, function, signaling regulation and even cancer. NleB and SseK are bacterial effector proteins and possess glycosyltransferase activity, even though they have different substrate preferences. NleB/SseKs transfer the GlcNAc sugar to an arginine residue of host proteins, leading to reduced