CRYSTAL STRUCTURE OF HUMAN PROTEIN PHOSPHATASE 2A

$143,176P41FY2001RRNIH

Stanford University, Stanford CA

Investigators

Linked publications & trials

Paper 37695261 Paper 37214971 Paper 37130087 Paper 36123347 Paper 36073854 Paper 35973205 Paper 35959919 Paper 35902572 Paper 35594401 Paper 35472493 Paper 35420470 Paper 35133175 Paper 35063097 Paper 34823974 Paper 34547292 Paper 33908775 Paper 33821273 Paper 33753488 Paper 33741910 Paper 33723266 Paper 33665861 Paper 33226796 Paper 33187988 Paper 32780051 Paper 32719366 Paper 32512156 Paper 32494617 Paper 32423902 Paper 32286284 Paper 32142641 Paper 32123169 Paper 31757767 Paper 31701135 Paper 31583886 Paper 31550535 Paper 31395658 Paper 31358584 Paper 31320619 Paper 31266803 Paper 31197138 Paper 31189111 Paper 30987231 Paper 30855230 Paper 30556652 Paper 30508304 Paper 30489586 Paper 30455349 Paper 30407190 Paper 30352853 Paper 30318466 Paper 30282808 Paper 30275500 Paper 29954862 Paper 29760050 Paper 29677513 Paper 29649442 Paper 29535379 Paper 29056481 Paper 28949128 Paper 28827308 Paper 28781082 Paper 28698372 Paper 28694323 Paper 28692802 Paper 28655912 Paper 28652405 Paper 28514451 Paper 28496149 Paper 28442575 Paper 28440794 Paper 28402848 Paper 28343996 Paper 28300169 Paper 28179428 Paper 28096352 Paper 28083542 Paper 28056108 Paper 27811937 Paper 27789737 Paper 27756898 Paper 27679816 Paper 27626829 Paper 27580719 Paper 27574710 Paper 27573242 Paper 27545823 Paper 27489265 Paper 27351594 Paper 27349805 Paper 27320962 Paper 27310336 Paper 27288442 Paper 27191344 Paper 27151871 Paper 27128252 Paper 27099162 Paper 27050127 Paper 27003615 Paper 26990311 Paper 26969531

Abstract

Protein phosphatase 2A (PP2A) is a serine/threonine-specific phosphatase that participates in cell cycle control, signal transduction and whose activity is altered during viral tumorigenesis. We wish to understand the role of PP2A in tumor formation by SV40 and polyoma viruses by analyzing the crystal structure of the regulatory A subunit of PP2A. At beamline 7-1 at SSRL we collected a 77% complete, native data set with 6.4% Rsym to 3.1 E. The difference synchrotron radiation makes is dramatic: it's high intensity and narrow collimation improves spatial resolution of the spots and increases diffraction by at least 2.4E over what we can achieve in our lab.

View original record on NIH RePORTER →