Crystal structure of the dual specificity protein phosphatase VHR

Science

Volumn 272, Issue 5266, 1996, Pages 1328-1331

  Yuvaniyama, Jirundon ^a   Denu, John M ^a   Dixon, Jack E ^a   Saper, Mark A ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME PHOSPHORYLATION; ENZYME SPECIFICITY; HUMAN; OPEN READING FRAME; PRIORITY JOURNAL; SIGNAL TRANSDUCTION; VACCINIA;

EID: 0029975476     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.272.5266.1328     Document Type: Article

References (38)

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17. free (32) was 25.4% (1867 reflections) for 2929 atoms (residues 8 to 185 in two VHR molecules, one sulfate, one Hepes, and 141 ordered water molecules). The root mean square deviation (rmsd) from ideal bonds and angles was 0.016 A and 1.7 Å, respectively. The rmsd between the two NCS-related molecules was 1.26 Å for all atoms and 0.82 Å for main chain atoms. The VHR coordinates are available from the Brookhaven Protein Data Bank as entry 1VHR.
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27. We used the secondary structure of VHR and the secondary structure predicted for CL100 and PAC-1 [B. Rost, C. Sander, R. Schneider, Comput. Appl. Biosci. 10, 53 (1994)] together with the CLUSTALV program [D. G. Higgins, A. J. Bleasby, R. Fuchs, ibid. 8, 189 (1992)] to construct a sequence alignment of the three DSPs. To locate the start of the catalytic domain in CL100, corresponding to the α1 helix in VHR, we scanned upstream terminus of the β1 strand for predicted helices in the CL100 sequence that had the best primary sequence alignment with VHR. The catalytic domains of CL100 and PAC-1 were predicted from the alignment to begin at residues 123 and 130, respectively.
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38. We thank M. Wishart for help with the CL100 and PAC-1 alignments and C. Yuvaniyama for technical support. Supported by the NIH (grant AI34095 to MAS. and grants DK18024 and DK18849 to J.E.D.), a National Research Service award to J.M.D. (GM17789), the University of Michigan Multipurpose Arthritis Center (NIH grant P60-AR20557), and Mitotix Inc. J.Y. is a scholar of the Thai Development and Promotion of Science and Technology Talents Project. M.A.S. is a Pew Scholar in the Biomedical Sciences.