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Lee, Changwook
Structural Biology of Cellular Biochemistry Lab
Research Interests
  • Cell biology, structural biology, protein biochemistry, membrane biology, cancer biology

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Structure of a peptide : N-glycanase-Rad23 complex: Insight into the deglycosylation for denatured glycoproteins

Cited 43 times inthomson ciCited 43 times inthomson ci
Title
Structure of a peptide : N-glycanase-Rad23 complex: Insight into the deglycosylation for denatured glycoproteins
Author
Lee, Jung-HoonChoi, Jung MinLee, ChangwookYi, Ki JoungCho, Yunje
Issue Date
2005-06
Publisher
NATL ACAD SCIENCES
Citation
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.102, no.26, pp.9144 - 9149
Abstract
In eukaryotes, misfolded proteins must be distinguished from correctly folded proteins during folding and transport processes by quality control systems. Yeast peptide:N-glycanase (yPNGase) specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists proteasome-mediated glycoprotein degradation by forming a complex with 26S proteasome through DNA repair protein, yRad23. Here, we describe the crystal structures of a yPNGase and XPC-binding domain of yRad23 (yRad23XBD, residues 238-309) complex and of a yPNGase-yRad23XBD complex bound to a caspase inhibitor, Z-VAD-fmk. yPNGase is formed with three domains, a core domain containing a Cys-His-Asp triad, a Zn-binding domain, and a Rad23-binding domain. Both N- and C-terminal helices of yPNGase interact with yRad23 through extensive hydrophobic interactions. The active site of yPNGase is located in a deep cleft that is formed with residues conserved in all PNGase members, and three sugar molecules are bound to this cleft. Complex structures in conjunction with mutational analyses revealed that the walls of the cleft block access to the active site of yPNGase by native glycoprotein, whereas the cleft is sufficiently wide to accommodate denatured glycoprotein, thus explaining the specificity of PNGase for denatured substrates.
URI
https://scholarworks.unist.ac.kr/handle/201301/9792
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=21544450264
DOI
10.1073/pnas.0502082102
ISSN
0027-8424
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