L
Leehyeon Kim
Researcher at Korea University
Publications - 15
Citations - 225
Leehyeon Kim is an academic researcher from Korea University. The author has contributed to research in topics: Degron & Chemistry. The author has an hindex of 7, co-authored 13 publications receiving 141 citations.
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Journal ArticleDOI
Insights into degradation mechanism of N-end rule substrates by p62/SQSTM1 autophagy adapter
Do Hoon Kwon,Ok Hyun Park,Leehyeon Kim,Yang Ouk Jung,Yeonkyoung Park,Hyeongseop Jeong,Jae-Kyung Hyun,Yoon Ki Kim,Hyun Kyu Song +8 more
TL;DR: Molecular insights into p62 N-end rule substrate recognition are provided by solving the structures of the p62 ZZ-domain in complex with various type 1 and type 2 degrons and also show the pH dependent oligomerization of p62.
Journal ArticleDOI
The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation of LC3 on the phagophore membrane
Do Hoon Kwon,Sulhee Kim,Yang Ouk Jung,Kyung Hye Roh,Leehyeon Kim,Byeong Won Kim,Seung Beom Hong,In Young Lee,Ju Han Song,Woo Cheol Lee,Eui Ju Choi,Kwang Yeon Hwang,Hyun Kyu Song +12 more
TL;DR: Based on the biochemical, structural, and cell-based analyses of RavZ and LC3, both distant flexible N- and C-terminal regions containing LC3-interacting region (LIR) motifs are important for substrate recognition.
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Structural and Biochemical Study of the Mono-ADP-Ribosyltransferase Domain of SdeA, a Ubiquitylating/Deubiquitylating Enzyme from Legionella pneumophila.
TL;DR: The mono-ADP-ribosyltransferase domain of SdeA is characterized and it is shown that it consists of two sub-domains termed mART-N and mart-C, which provide insight into the unusual ubiquitylation mechanism of S deA and expand knowledge on the structure-function of mono- ADP- ribosyl transferases.
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A novel conformation of the LC3-interacting region motif revealed by the structure of a complex between LC3B and RavZ.
Do Hoon Kwon,Leehyeon Kim,Byeong Won Kim,Jun Hoe Kim,Kyung Hye Roh,Eui Ju Choi,Hyun Kyu Song +6 more
TL;DR: The tandem LIR motifs located in the N-terminal region of RavZ adopt a novel β-sheet conformation and thus provide specific ionic interactions with LC3B in addition to canonical hydrophobic plugged-in interactions, which broaden the understanding of the functional repertoire of Lir motifs in autophagy.
Journal ArticleDOI
Aminopeptidases trim Xaa-Pro proteins, initiating their degradation by the Pro/N-degron pathway.
TL;DR: In this paper, specific aminopeptidases function as components of the Pro/N-degron pathway by removing Nt-Ala or NtSer and yielding NtPro, which can be recognized by Gid4-GID.