TY - JOUR
T1 - Backbone assignment of the UHM domain of Puf60 free and bound to five ligands
AU - Corsini, Lorenzo
AU - Sattler, Michael
N1 - Funding Information:
Acknowledgments This work was supported by the Deutsche Forschungsgemeinschaft (Sa 823/5) and EC (3D Repertoire, LSHG-CT–2005–512028).
PY - 2008/12
Y1 - 2008/12
N2 - U2AF homology motifs (UHM) are protein domains that bind peptidic UHM ligand motifs (ULM) and thus form an intricate network of interactions involved in splicing regulation. Here, we report the backbone assignment of the UHM domain of the splicing factor Puf60 as well as 1H, 15N chemical shifts upon binding of the ULM peptides U2AF 65 (85-112), SF1 (1-25), SF3b155 (194-229), SF3b155 (317-357), and Prp16 (201-238).
AB - U2AF homology motifs (UHM) are protein domains that bind peptidic UHM ligand motifs (ULM) and thus form an intricate network of interactions involved in splicing regulation. Here, we report the backbone assignment of the UHM domain of the splicing factor Puf60 as well as 1H, 15N chemical shifts upon binding of the ULM peptides U2AF 65 (85-112), SF1 (1-25), SF3b155 (194-229), SF3b155 (317-357), and Prp16 (201-238).
KW - Alternative splicing
KW - Chemical shift perturbation
KW - FBP interacting repressor
KW - Splicing
KW - UHM
KW - ULM
UR - http://www.scopus.com/inward/record.url?scp=68849100480&partnerID=8YFLogxK
U2 - 10.1007/s12104-008-9123-7
DO - 10.1007/s12104-008-9123-7
M3 - Article
C2 - 19636907
AN - SCOPUS:68849100480
SN - 1874-2718
VL - 2
SP - 211
EP - 214
JO - Biomolecular NMR Assignments
JF - Biomolecular NMR Assignments
IS - 2
ER -