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- Title
The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites.
- Authors
Brands, J H; Maassen, J A; van Hemert, F J; Amons, R; Möller, W
- Abstract
The primary structure of the alpha subunit of elongation factor 1 (EF-1 alpha) from human MOLT 4 cells was determined by cDNA sequencing. The data show that the conservation of the amino acid sequence is more than 80% when compared with yeast and Artemia EF-1 alpha. An inventory of amino acid sequences around the guanine-nucleotide-binding site in elongation factor Tu from Escherichia coli and homologous amino acid sequences in G proteins, initiation and elongation factors and proteins from the RAS family shows two regions containing conserved sequence elements. Region I has the sequence apolar-Xaa-Xaa-Xaa-Gly-Xaa-Xaa-Yaa-Xaa-Gly-LYs-Thr(Ser)- -Xaa-Xaa-Xaa-Xaa-X-apolar. Except for RAS proteins, Yaa is always an acidic amino acid residue. Region II is characterized by the invariant sequence apolar-apolar-Xaa-Xaa-Asn-Lys-Xaa-Asp. In order to facilitate sequence comparison we have used a graphic display, which is based on the hydrophilicity values of individual amino acids in a sequence.
- Publication
European journal of biochemistry, 1986, Vol 155, Issue 1, p167
- ISSN
0014-2956
- Publication type
Journal Article
- DOI
10.1111/j.1432-1033.1986.tb09472.x