Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family.
The human dual-specificity protein phosphatase 18 (DSP18) gene and its protein product have recently been characterized. Like most DSPs, DSP18 displays dephosphorylating activity towards both phosphotyrosine and phosphothreonine residues. However, DSP18 is distinct from other known DSPs in terms of the existence of approximately 30 residues at the C-terminus of the catalytic domain and an unusual optimum activity profile at 328 K. The crystal structure of human DSP18 has been determined at 2.0 A resolution. The catalytic domain of DSP18 adopts a fold similar to that known for other DSP structures. Although good alignments are found with other DSPs, substantial differences are also found in the regions surrounding the active site, suggesting that DSP18 constitutes a unique structure with a distinct substrate specificity. Furthermore, the residues at the C-terminus fold into two antiparallel beta-strands and participate in extensive interactions with the catalytic domain, explaining the thermostability of DSP18.
Jeong
Dae Gwin
DG
Systemic Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology, 52 Eoeun-Dong, Yuseong-Gu, Daejeon 305-333, South Korea.
Cho
Yoon Hea
YH
Yoon
Tae Sung
TS
Kim
Jae Hoon
JH
Son
Jeong Hee
JH
Ryu
Seong Eon
SE
Kim
Seung Jun
SJ
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001665:Binding Sites; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D054637:Dual-Specificity Phosphatases; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry* / Q000145:classification; D016415:Sequence Alignment
C473895:DUSP18 protein, human; D054637:Dual-Specificity Phosphatases; D017027:Protein Tyrosine Phosphatases