CRYSTAL STRUCTURE OF STAT4 N TERMINAL DOMAIN

$13,750P41FY2000RRNIH

Cornell University Ithaca, Ithaca NY

Investigators

Linked publications & trials

Paper 39016322 Paper 38659970 Paper 35979957 Paper 32571875 Paper 30983160 Paper 30341174 Paper 29945973 Paper 29414699 Paper 29352104 Paper 29159828 Paper 28111017 Paper 27923041 Paper 27295975 Paper 26870381 Paper 26859324 Paper 26768709 Paper 26294765 Paper 26224628 Paper 26092730 Paper 25869669 Paper 25620000 Paper 25463020 Paper 25422459 Paper 25354681 Paper 25225968 Paper 25117499 Paper 25006264 Paper 24704217 Paper 24662985 Paper 24549644 Paper 24098668 Paper 24095061 Paper 23978130 Paper 23965125 Paper 23843460 Paper 23695562 Paper 23614004 Paper 23524536 Paper 23395181 Paper 23373518 Paper 23365681 Paper 23342998 Paper 23334294 Paper 23273425 Paper 23254651 Paper 23079036 Paper 23066817 Paper 23051056 Paper 23000721 Paper 23000384 Paper 23000382 Paper 22948911 Paper 22942283 Paper 22872863 Paper 22849347 Paper 22841292 Paper 22767592 Paper 22727814 Paper 22707706 Paper 22637474 Paper 22607171 Paper 22509071 Paper 22505402 Paper 22496338 Paper 22496238 Paper 22411556 Paper 22315069 Paper 22292922 Paper 22281741 Paper 22245575 Paper 22167801 Paper 22160671 Paper 22154808 Paper 22119916 Paper 22076378 Paper 22049338 Paper 21992006 Paper 21972022 Paper 21965687 Paper 21947008 Paper 21931220 Paper 21931214 Paper 21917284 Paper 21904032 Paper 21900159 Paper 21892836 Paper 21887263 Paper 21873985 Paper 21846932 Paper 21843643 Paper 21822345 Paper 21788477 Paper 21786812 Paper 21697603 Paper 21652723 Paper 21647365 Paper 21640829 Paper 21636905 Paper 21592962 Paper 21549712

Abstract

We collected an outstanding data set from a crystals of the dual specificity phosphatase VHR complexed with vanadate. The data extended to at least 1.6 [unreadable], and had an Rsym of 3.5% to 1.8 [unreadable]. This structure recently has been solved and provides insights into the transition state of phosphate hydrolysis. Several data sets were also collected from the catalytic domain of the LAR receptor tyrosine phosphatase. Data collected from frozen crystals of an anti-DNA Fab fragment are now being used to refine the structure of this antibody.

View original record on NIH RePORTER →