Detailed Information

Cited 0 time in webofscience Cited 0 time in scopus
Metadata Downloads

The family-wide structure and function of human dual-specificity protein phosphatases

Full metadata record
DC Field Value Language
dc.contributor.authorJeong, Dae Gwin-
dc.contributor.authorWei, Chun Hua-
dc.contributor.authorKu, Bonsu-
dc.contributor.authorJeon, Tae Jin-
dc.contributor.authorPham Ngoc Chien-
dc.contributor.authorKim, Jae Kwan-
dc.contributor.authorPark, So Ya-
dc.contributor.authorHwang, Hyun Sook-
dc.contributor.authorRyu, Sun Young-
dc.contributor.authorPark, Hwangseo-
dc.contributor.authorKim, Deok-Soo-
dc.contributor.authorKim, Seung Jun-
dc.contributor.authorRyu, Seong Eon-
dc.date.accessioned2022-07-16T06:10:49Z-
dc.date.available2022-07-16T06:10:49Z-
dc.date.created2021-05-12-
dc.date.issued2014-02-
dc.identifier.issn2059-7983-
dc.identifier.urihttps://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/160742-
dc.description.abstractDual-specificity protein phosphatases (DUSPs), which dephosphorylate both phosphoserine/threonine and phosphotyrosine, play vital roles in immune activation, brain function and cell-growth signalling. A family-wide structural library of human DUSPs was constructed based on experimental structure determination supplemented with homology modelling. The catalytic domain of each individual DUSP has characteristic features in the active site and in surface-charge distribution, indicating substrate-interaction specificity. The active-site loop-to-strand switch occurs in a subtype-specific manner, indicating that the switch process is necessary for characteristic substrate interactions in the corresponding DUSPs. A comprehensive analysis of the activity inhibition profile and active-site geometry of DUSPs revealed a novel role of the active-pocket structure in the substrate specificity of DUSPs. A structure-based analysis of redox responses indicated that the additional cysteine residues are important for the protection of enzyme activity. The family-wide structures of DUSPs form a basis for the understanding of phosphorylation-mediated signal transduction and the development of therapeutics.-
dc.language영어-
dc.language.isoen-
dc.publisherINT UNION CRYSTALLOGRAPHY-
dc.titleThe family-wide structure and function of human dual-specificity protein phosphatases-
dc.typeArticle-
dc.contributor.affiliatedAuthorKim, Deok-Soo-
dc.contributor.affiliatedAuthorRyu, Seong Eon-
dc.identifier.doi10.1107/S1399004713029866-
dc.identifier.scopusid2-s2.0-84894120177-
dc.identifier.wosid000331554500021-
dc.identifier.bibliographicCitationACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, v.70, pp.421 - 435-
dc.relation.isPartOfACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY-
dc.citation.titleACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY-
dc.citation.volume70-
dc.citation.startPage421-
dc.citation.endPage435-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.relation.journalResearchAreaCrystallography-
dc.relation.journalWebOfScienceCategoryBiochemical Research Methods-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.relation.journalWebOfScienceCategoryCrystallography-
dc.subject.keywordPlusCRYSTAL-STRUCTURE-
dc.subject.keywordPlusCATALYTIC DOMAIN-
dc.subject.keywordPlusKINASE PHOSPHATASE-
dc.subject.keywordPlusTYROSINE PHOSPHATASES-
dc.subject.keywordPlusREDOX REGULATION-
dc.subject.keywordPlusBINDING DOMAIN-
dc.subject.keywordPlusCELL-GROWTH-
dc.subject.keywordPlusMAP-
dc.subject.keywordPlusACTIVATION-
dc.subject.keywordPlusSUBSTRATE-
dc.subject.keywordAuthordual-specificity protein phosphatases-
dc.subject.keywordAuthorDUSPs-
dc.subject.keywordAuthorprotein tyrosine phosphatases-
dc.identifier.urlhttp://scripts.iucr.org/cgi-bin/paper?S1399004713029866-
Files in This Item
Go to Link
Appears in
Collections
서울 공과대학 > 서울 생명공학과 > 1. Journal Articles
서울 공과대학 > 서울 기계공학부 > 1. Journal Articles

qrcode

Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.

Related Researcher

Researcher Ryu, Seong Eon photo

Ryu, Seong Eon
COLLEGE OF ENGINEERING (DEPARTMENT OF BIOENGINEERING)
Read more

Altmetrics

Total Views & Downloads

BROWSE