The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites.
作者： Jolanda H. G. M. BRANDS , J. Antonie MAASSEN , Formijn J. HEMERT , Reinout AMONS , Wim MOLLER
DOI: 10.1111/J.1432-1033.1986.TB09472.X
关键词:
摘要: The primary structure of the α subunit elongation factor 1 (EF- 1α) from human MOLT 4 cells was determined by cDNA sequencing. data show that conservation amino acid sequence is more than 80% when compared with yeast and Artemia EF-1α. An inventory sequences around guanine-nucleotide-binding site in Tu Escherichia coli homologous G proteins, initiation factors proteins RAS family shows two regions containing conserved seqence elements. Region I has apolar-Xaa-Xaa-Xaa-Gly-Xaa-Xaa-Yaa-Xaa-Gly-Lys-Thr(Ser)-Xaa-Xaa-Xaa-Xaa-X-apolar. Except for Yaa always an acidic residue. Region II characterized invariant apolar-apolar-Xaa-Xaa-Asn-Lys-Xaa-Asp. In order to facilitate comparison we have used a graphic display, which based on hydrophilicity values individual acids sequence.
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