caa a22 4500 477136664 CHVBK 20180405111720.0 cr unu---uuuuu 170330e19970201xx s 000 0 eng 10.1023/A:1018636018243 doi (NATIONALLICENCE)springer-10.1023/A:1018636018243 Resonance assignments, secondary structure and topology of leukaemia inhibitory factor in solution [Elektronische Daten] [Mark Hinds, Till Maurer, Jian-Guo Zhang, Nicos Nicola, and Norton] The chemical shift assignments and secondary structure of a murine-human chimera,MH35, of leukaemia inhibitory factor (LIF), a 180-residue protein of molecular mass 20 kDa,have been determined from multidimensional heteronuclear NMR spectra acquired on auniformly 13C,15N-labelled sample. Secondary structure elements were defined on the basisof chemical shifts, NH-CαH coupling constants, medium-range NOEs and the location ofslowly exchanging amide protons. The protein contains four α-helices, the relativeorientations of which were determined on the basis of long-range, interhelical NOEs. The fourhelices are arranged in an up-up-down-down orientation, as found in other four-helical bundlecytokines. The overall topology of MH35-LIF is similar to that of the X-ray crystallographicstructure for murine LIF [Robinson et al. (1994) Cell, 77, 1101-1116]. Differencesbetween the X-ray structure and the solution structure are evident in the N-terminal tail, wherethe solution structure has a trans-Pro17 compared with the cis-Pro17 found in the crystalstructure and the small antiparallel β-sheet encompassing residues in the N-terminus andCD loop in the crystal structure is less stable. Kluwer Academic Publishers, 1997 Cytokine nationallicence Leukaemia inhibitory factor nationallicence Isotope labelling nationallicence Heteronuclear NMR nationallicence Chemical shift assignments nationallicence Helices nationallicence Hinds Mark Biomolecular Research Institute, 343 Royal Parade, 3052, Parkville, VIC, Australia aut Maurer Till Biomolecular Research Institute, 343 Royal Parade, 3052, Parkville, VIC, Australia aut Zhang Jian-Guo The Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, 3050, Melbourne, VIC, Australia aut Nicola Nicos The Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, 3050, Melbourne, VIC, Australia aut Norton and Biomolecular Research Institute, 343 Royal Parade, 3052, Parkville, VIC, Australia aut Journal of Biomolecular NMR Kluwer Academic Publishers 9/2(1997-02-01), 113-126 0925-2738 9:2<113 1997 9 10858 https://doi.org/10.1023/A:1018636018243 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018636018243 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Hinds Mark Biomolecular Research Institute, 343 Royal Parade, 3052, Parkville, VIC, Australia aut NATIONALLICENCE 700 1- Maurer Till Biomolecular Research Institute, 343 Royal Parade, 3052, Parkville, VIC, Australia aut NATIONALLICENCE 700 1- Zhang Jian-Guo The Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, 3050, Melbourne, VIC, Australia aut NATIONALLICENCE 700 1- Nicola Nicos The Walter and Eliza Hall Institute of Medical Research, P.O. Royal Melbourne Hospital, 3050, Melbourne, VIC, Australia aut NATIONALLICENCE 700 1- Norton and Biomolecular Research Institute, 343 Royal Parade, 3052, Parkville, VIC, Australia aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Kluwer Academic Publishers 9/2(1997-02-01), 113-126 0925-2738 9:2<113 1997 9 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer