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Lee, Changwook
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dc.citation.endPage 9149 -
dc.citation.number 26 -
dc.citation.startPage 9144 -
dc.citation.title PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA -
dc.citation.volume 102 -
dc.contributor.author Lee, Jung-Hoon -
dc.contributor.author Choi, Jung Min -
dc.contributor.author Lee, Changwook -
dc.contributor.author Yi, Ki Joung -
dc.contributor.author Cho, Yunje -
dc.date.accessioned 2023-12-22T10:36:24Z -
dc.date.available 2023-12-22T10:36:24Z -
dc.date.created 2014-10-14 -
dc.date.issued 2005-06 -
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. -
dc.identifier.bibliographicCitation PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.102, no.26, pp.9144 - 9149 -
dc.identifier.doi 10.1073/pnas.0502082102 -
dc.identifier.issn 0027-8424 -
dc.identifier.scopusid 2-s2.0-21544450264 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/9792 -
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=21544450264 -
dc.identifier.wosid 000230191400012 -
dc.language 영어 -
dc.publisher NATL ACAD SCIENCES -
dc.title Structure of a peptide : N-glycanase-Rad23 complex: Insight into the deglycosylation for denatured glycoproteins -
dc.type Article -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordAuthor deep cleft -
dc.subject.keywordAuthor PNGase -
dc.subject.keywordAuthor zinc-metalloenzyme -
dc.subject.keywordPlus PEPTIDE-N-GLYCANASE -
dc.subject.keywordPlus ENDOPLASMIC-RETICULUM -
dc.subject.keywordPlus CRYSTAL-STRUCTURE -
dc.subject.keywordPlus DNA-REPAIR -
dc.subject.keywordPlus CYTOPLASMIC PEPTIDE -
dc.subject.keywordPlus PROTEIN-DEGRADATION -
dc.subject.keywordPlus YEAST PEPTIDE -
dc.subject.keywordPlus RAD23 -
dc.subject.keywordPlus RESOLUTION -
dc.subject.keywordPlus MECHANISM -

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