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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

Authors 

Dae Gwin JeongTae-Sung YoonJ H KimM Y ShimSuk-Kyeong JungJeong Hee SonSeong Eon RyuSeung Jun Kim

Publisher 

Elsevier

Issue Date 

2006

Citation 

Journal of Molecular Biology, vol. 360, no. 5, pp. 946-955

Keywords 

constitutive activityexperimental autoimmune encephalomyelitismitogen-activated protein kinase phosphatase 5protein tyrosine phosphatasesubstrate induced activationmitogen activated protein kinase 7phosphatasecrystal structureenzyme active site

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.

ISSN 

0022-2836

Link 

http://dx.doi.org/10.1016/j.jmb.2006.05.059

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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