Premium
Homology versus analogy: possible evolutionary relationship of immunoglobulins, cupredoxins, and Cu,Zn‐superoxide dismutase
Author(s) -
Stevens Fred J.
Publication year - 2008
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.861
Subject(s) - homology (biology) , superoxide dismutase , analogy , antibody , homology modeling , biology , evolutionary biology , function (biology) , protein structure , computational biology , structural similarity , genetics , biochemistry , enzyme , gene , epistemology , philosophy
The ‘immunoglobulin‐like’ fold is one of most common structural motifs observed in proteins. This topology is found in more than 80 superfamilies of proteins, including Cu,Zn‐superoxide dismutase (SOD) and cupredoxin. Evolutionary relationships have not been identified, but may exist. The challenge remains, therefore, of resolving the issue of whether the diverse distribution of the fold is accounted for by divergent evolution of function or convergent evolution of structure following multiple independent origins of function. Since the early studies that revealed conformational similarity of immunoglobulins and other proteins, the number of primary structures available for comparison has dramatically increased and new computational approaches for analysis of sequences have been developed. It now appears that a hypothesis of a common evolutionary origin for cupredoxins, Cu,Zn‐SOD, and immunoglobulins may be credible. The distinction between protein homology and protein analogy is fundamental. The immunoglobulin‐like fold may represent a robust system within which to examine again the issue of protein homology versus analogy. Copyright © 2007 John Wiley & Sons, Ltd.