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Short inverse complementary amino acid sequences generate protein complexity.

Daniel J Goldstein·Christian Fondrat·Florence Muri·Gregory Nuel·Patricia Saragueta·Anne-Sophie Tocquet·Bernard Prum
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Abstract

Inversions of short genomic sequences play a central role in the generation of protein complexity. More than half of the 1300 motifs registered in ProSite have protein inverse complementary sequences (princoms) among proteins registered in SwissProt. The observed number of princoms occurrences exceeds by far the expected number (p < 10(-10)). Princoms often endow their host proteins with a whole new range of biochemical and physiological capabilities, including the possibility of intramolecular and intermolecular disulfide bond formation. These results support the idea that, like the duplications, the inversions of small genomic fragments have been a fundamental mechanism for shaping genomes.

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Amino Acid MotifsAmino Acid SequenceAnimalsApoptosisBase SequenceDNADatabases, ProteinDisulfidesEvolution, MolecularGenesHemoglobinsHumansImmunoglobulin GMathematicsProtein Structure, TertiaryProteinsvon Willebrand FactorJournal Article

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Daniel J Goldstein, Christian Fondrat, Florence Muri, Gregory Nuel, Patricia Saragueta, Anne-Sophie Tocquet, Bernard Prum. 2003. Short inverse complementary amino acid sequences generate protein complexity.. https://doi.org/10.1016/s1631-0691(03)00077-5

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