1zzw
From Proteopedia
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Crystal Structure of catalytic domain of Human MAP Kinase Phosphatase 5
Overview
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 A. 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.
About this Structure
1ZZW is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of human MAP kinase phosphatase 5: structural insight into constitutively active phosphatase., Jeong DG, Yoon TS, Kim JH, Shim MY, Jung SK, Son JH, Ryu SE, Kim SJ, J Mol Biol. 2006 Jul 28;360(5):946-55. Epub 2006 Jun 9. PMID:16806267
Page seeded by OCA on Thu Feb 21 16:20:42 2008
Categories: Homo sapiens | Single protein | Jeong, D G. | Jeong, S K. | Kim, J H. | Kim, S J. | Ryu, S E. | Shim, M Y. | Son, J H. | Yoon, T S. | EDO | SO4 | Mkp | Phosphatase | Ptp
