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dc.contributor.author류성언-
dc.date.accessioned2017-01-12T06:13:54Z-
dc.date.available2017-01-12T06:13:54Z-
dc.date.issued2015-06-
dc.identifier.citationBiodesign, v. 3, NO 2, Page. 111-116en_US
dc.identifier.issn2288-6982-
dc.identifier.issn2288-7105-
dc.identifier.urihttp://www.bdjn.org/inc_function/File_Download.php?File_In_Type=Sub&File_Field=j_sub_pdf&j_filenum=41-
dc.identifier.urihttp://hdl.handle.net/20.500.11754/25110-
dc.description.abstractThe activity of cellular signaling proteins modulates cellular processes such as cell growth, immune responses, and neuronal development. Dual specificity phosphatases (DUSPs), which constitute a subfamily of protein tyrosine phosphatases (PTPs), are potential targets for therapeutic development. Recently, allosteric inhibitors of PTPs have shown promising results with regard to their potency, selectivity and membrane permeability. However, detailed understanding of the activity regulation of PTPs is limited. Thus, we determined crystal structures of activity-modulating mutants of DUSP19 for which strongly-diffracting crystals are available. One allosteric residue (Ile 187) and two active site residues (Ser 150 and Arg 156) were mutated to alanine. High-resolution crystal structure determination and enzyme kinetics analysis of the three mutants revealed that the mutations resulted in rearrangements in allosteric and local structures. In particular, cavityfilling rearrangements in the I187A mutant were conveyed to the active site, leading to allosteric regulation of enzyme activity.en_US
dc.description.sponsorshipThis work was supported by the next generation applied-omics project (NRF-2011-0030030) and a Hanyang University internal grant.en_US
dc.language.isoenen_US
dc.publisherKorean Society for Structural Biologyen_US
dc.titleStructural analysis of activity-modulating mutations of DUSP19en_US
dc.typeArticleen_US
dc.relation.no2-
dc.relation.volume3-
dc.relation.page111-116-
dc.relation.journalBiodesign-
dc.contributor.googleauthorJeon, Tae Jin-
dc.contributor.googleauthorNam, Kyoung Tae-
dc.contributor.googleauthorRyu, Seong Eon-
dc.relation.code2014042555-
dc.sector.campusS-
dc.sector.daehakCOLLEGE OF ENGINEERING[S]-
dc.sector.departmentDEPARTMENT OF BIOENGINEERING-
dc.identifier.pidryuse-
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COLLEGE OF ENGINEERING[S](공과대학) > BIOENGINEERING(생명공학과) > Articles
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