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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

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dc.contributor.author Lee, Jung-Hoon ko
dc.contributor.author Choi, Jung Min ko
dc.contributor.author Lee, Changwook ko
dc.contributor.author Yi, Ki Joung ko
dc.contributor.author Cho, Yunje ko
dc.date.available 2015-01-05T00:02:16Z -
dc.date.created 2014-10-14 ko
dc.date.issued 2005-06 ko
dc.identifier.citation PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.102, no.26, pp.9144 - 9149 ko
dc.identifier.issn 0027-8424 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/9792 -
dc.description.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. ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher NATL ACAD SCIENCES ko
dc.title Structure of a peptide : N-glycanase-Rad23 complex: Insight into the deglycosylation for denatured glycoproteins ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-21544450264 ko
dc.identifier.wosid 000230191400012 ko
dc.type.rims ART ko
dc.description.wostc 43 *
dc.description.scopustc 43 *
dc.date.tcdate 2015-12-28 *
dc.date.scptcdate 2015-11-04 *
dc.identifier.doi 10.1073/pnas.0502082102 ko
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=21544450264 ko
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