Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: structural insight into constitutively active phosphatase = 인간MAP카이네이즈 탈인산화효소 5 활성화 영역의 결정화구조

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Title
Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: structural insight into constitutively active phosphatase = 인간MAP카이네이즈 탈인산화효소 5 활성화 영역의 결정화구조
Author(s)
Dae Gwin JeongTae-Sung Yoon; J H Kim; M Y Shim; Suk-Kyeong Jung; Jeong Hee Son; Seong Eon Ryu; Seung Jun Kim
Bibliographic Citation
Journal of Molecular Biology, vol. 360, no. 5, pp. 946-955
Publication Year
2006
Abstract
MAP kinase phosphatase 5 (MKP5) is a member of the mitogen-activated protein kinase phosphatase (MKP) family and selectively dephosphorylates JNK and p38. We have determined the crystal structure of the catalytic domain of human MKP5 (MKP5-C) to 1.6 ?. In previously reported MKP-C structures, the residues that constitute the active site are seriously deviated from the active conformation of protein tyrosine phosphatases (PTPs), which are accompanied by low catalytic activity. High activities of MKPs are achieved by binding their cognate substrates, representing substrate-induced activation. However, the MKP5-C structure adopts an active conformation of PTP even in the absence of its substrate binding, which is consistent with the previous results that MKP5 solely possesses the intrinsic activity. Further, we identify a sequence motif common to the members of MKPs having low catalytic activity by comparing structures and sequences of other MKPs. Our structural information provides an explanation of constitutive activity of MKP5 as well as the structural insight into substrate-induced activation occurred in other MKPs.
Keyword
constitutive activityexperimental autoimmune encephalomyelitismitogen-activated protein kinase phosphatase 5protein tyrosine phosphatasesubstrate induced activation
ISSN
0022-2836
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.jmb.2006.05.059
Type
Article
Appears in Collections:
Division of Research on National Challenges > Infectious Disease Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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