DSpace Собрание: Biology Direct is an open access, peer reviewed journal devoted to the biochemistry, genetics, cell, molecular, and computational biology of organisms and cells. Biology Direct is an open access, peer reviewed journal devoted to the biochemistry, genetics, cell, molecular, and computational biology of organisms and cells. http://hdl.handle.net/20.500.12701/2147 2024-05-03T12:29:10Z 2024-05-03T12:29:10Z Conserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are rationalized as ligand binding sites Eisenhaber, Birgit Sinha, Swati Jadalanki, Chaitanya K. Shitov, Vladimir A. Tan, Qiao Wen Sirota, Fernanda L. Eisenhaber, Frank http://hdl.handle.net/20.500.12701/2148 2022-06-25T06:33:39Z 2021-01-12T00:00:00Z Название: Conserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are rationalized as ligand binding sites Авторы: Eisenhaber, Birgit; Sinha, Swati; Jadalanki, Chaitanya K.; Shitov, Vladimir A.; Tan, Qiao Wen; Sirota, Fernanda L.; Eisenhaber, Frank Краткий осмотр (реферат): The human proteins TMTC1, TMTC2, TMTC3 and TMTC4 have been experimentally shown to be components of a new O-mannosylation pathway. Their own mannosyl-transferase activity has been suspected but their actual enzymatic potential has not been demonstrated yet. So far, sequence analysis of TMTCs has been compromised by evolutionary sequence divergence within their membrane-embedded N-terminal region, sequence inaccuracies in the protein databases and the difficulty to interpret the large functional variety of known homologous proteins (mostly sugar transferases and some with known 3D structure). 2021-01-12T00:00:00Z