1985
DOI: 10.1073/pnas.82.24.8597
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Multiple-alphabet amino acid sequence comparisons of the immunoglobulin kappa-chain constant domain.

Abstract: We compare the amino acid sequences of the constant domains of the immunoglobulin Kc chain of human, mouse, and rabbit by using four classification schemes ("alphabets") of the 20 amino acids based on their chemical, functional, charge, and structural properties. The comparison reveals three regions of pronounced similarity across the three species, independent of allotype. Two of these regions (residues 65-73 and 99-103) entail a high degree of identity at the DNA level and are distinguished from the rest of … Show more

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Cited by 37 publications
(12 citation statements)
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“…Therefore, we aligned and compared the amino acid sequences of these two proteins and noted that there were 28 differences. When these amino acids are grouped according to their chemical composition (41), 17 of the 28 differences are not conserved (Fig. 4A).…”
Section: Resultsmentioning
confidence: 99%
“…Therefore, we aligned and compared the amino acid sequences of these two proteins and noted that there were 28 differences. When these amino acids are grouped according to their chemical composition (41), 17 of the 28 differences are not conserved (Fig. 4A).…”
Section: Resultsmentioning
confidence: 99%
“…Other models based on observed sequence variability in large alignments of homologous protein sequences, such as the BLOSUM family [5], have proven popular and successful. Karlin and Ghandour [6] and George, Barker, and Hunt [7] proposed methods of weighting differences based on chemical, functional, charge and structural properties of amino acids and computing replacement probabilities based on the similarity of the involved residues. Doolittle's group proposed substitution matrices based on amino acid structural similarities combined with the ease of genetic interchange [8], while Stanfel added information pertaining to biochemical properties to inform the probability of amino acid interchangeability [9].…”
Section: Introductionmentioning
confidence: 99%
“…(c) THM1 sequence encompassing the aln mutation is highly conserved across species. In the C. elegans and C. reinhardtii orthologs, the substitution of glutamine by arginine is predicted to be a structurally conservative amino acid substitution 45 . The start methionine is shown for Mus musculus, Bos taurus, Homo sapiens and Gallus gallus orthologs.…”
Section: Supplementary Materialsmentioning
confidence: 99%