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Author(s): William B. McKinnon (corresponding author) [1]; Francis Nimmo [2]; Teresa Wong [1]; Paul M. Schenk [3]; Oliver L. White [4]; J. H. Roberts [5]; J. M. Moore [4]; J. [...]

Author(s): Douglas P. Hamilton (corresponding author) [1]; S. A. Stern [2]; J. M. Moore [3]; L. A. Young [2]; the New Horizons Geology, Geophysics & Imaging Theme Team Plutos Sputnik [...]

Author(s): F. Nimmo (corresponding author) [1]; D. P. Hamilton [2]; W. B. McKinnon [3]; P. M. Schenk [4]; R. P. Binzel [5]; C. J. Bierson [1]; R. A. Beyer [6]; [...]

Author(s): William B. McKinnon; Francis Nimmo; Teresa Wong; Paul M. Schenk; Oliver L. White; J. H. Roberts; J. M. Moore; J. R. Spencer; A. D. Howard; O. M. Umurhan; S. [...]

Large regions of the jovian moon Ganymede have been resurfaced, but the means has been unclear. Suggestions have ranged from volcanic eruptions of liquid water or solid ice to tectonic deformation, but definitive high-resolution morphological evidence has been lacking. Here we report digital elevation models of parts of the surface of Ganymede, derived from stereo pairs combining data from the Voyager and Galileo spacecraft, which reveal bright, smooth terrains that lie at roughly constant elevations 100 to 1,000 metres below the surrounding rougher terrains. These topographic data, together with new images that show fine-scale embayment and burial of older features, indicate that the smooth terrains were formed by flooding of shallow structural troughs by low-viscosity water-ice lavas. The oldest and most deformed areas (the 'reticulate' terrains) in general have the highest relative elevations, whereas units of the most common resurfaced type--the grooved terrain--lie at elevations between those of the smooth and reticulate terrains. Bright terrain, which accounts for some two-thirds of the surface, probably results from a continuum of processes, including crustal rifting, shallow flooding and groove formation. Volcanism plays an integral role in these processes, and is consistent with partial melting of Ganymede's interior.

The major FK506 binding protein (FKBP, relative molecular mass approximately 11,800; Mr 11.8K) and cyclophilin (Mr approximately 17K) belong to a class of proteins termed immunophilins. Although unrelated at the amino-acid sequence level, they both possess peptidyl-prolyl cis-trans isomerase activities which are inhibited by immunosuppressants that block signal transduction pathways leading to T-lymphocyte activation. FK506 and rapamycin strongly inhibit the peptidyl-prolyl cis-trans isomerase activity of FKBP, whereas cyclosporin A inhibits that of cyclophilin. The significance of this enzyme activity and the role of the immunophilins in immunoregulation is unknown. To understand better the function of the immunophilins and their interaction with inhibitors, we are investigating the solution structures of FKBP and FKBP-inhibitor complexes by multidimensional NMR methods. Here we report the solution conformation of FKBP, as generated by NMR, distance geometry and molecular dynamics methods. The regular secondary structure of FKBP is composed mainly of beta sheet (approximately 35%) with little helical structure (less than 10%). The hydrophobic core of the molecule, containing the buried side chains of six of the protein's nine aromatic amino acids, is enclosed by a five-stranded antiparallel beta sheet on one side, a loop and a short helix at residues 51-56 and 57-65, and an aperiodic loop at residues 81-95. Examination of the structure suggests a possible site of interaction with FK506.