Open AccessHomologies and anomalies in primary structural patterns of nucleotide binding proteins
Author(s) -
ARGOS Patrick,
LEBERMAN Reuben
Publication year - 1985
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1985.tb09244.x
Subject(s) - homology (biology) , nucleotide , computational biology , protein primary structure , biology , nucleic acid sequence , genetics , sequence homology , sequence (biology) , amino acid residue , sequence alignment , binding site , conserved sequence , homology modeling , peptide sequence , amino acid , biochemistry , gene , enzyme
In searches for homology among nucleotide binding proteins, recent reports have described primary structure alignments for stretches of 30 or so amino acid residues among a variety of proteins including the ras and src oncogene products. The significance of these sequence matches has been tested by searching in available data banks for certain conserved residue patterns resulting from the alignments. The tests suggest that alignments over these limited stretches are not necessarily justifiable and any implications for residues involved in nucleotide binding must be viewed with caution.