Correlating structure and function during the evolution of fibrinogen-related domains.

ABSTRACT: Fibrinogen-related domains (FReDs) are found in a variety of animal proteins with widely different functions, ranging from non-self recognition to clot formation. All appear to have a common surface where binding of one sort or other occurs. An examination of 19 completed animal genomes--including a sponge and sea anemone, six protostomes, and 11 deuterostomes--has allowed phylogenies to be constructed that show where various types of FReP (proteins containing FReDs) first made their appearance. Comparisons of sequences and structures also reveal particular features that correlate with function, including the influence of neighbor-domains. A particular set of insertions in the carboxyl-terminal subdomain was involved in the transition from structures known to bind sugars to those known to

SUBMITTER: Doolittle RF 

PROVIDER: S-EPMC3575912 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature