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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/PAG_BACAN PAG_BACAN]] One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. PA binds to a receptor (ATR) in sensitive eukaryotic cells, thereby facilitating the translocation of the enzymatic toxin components, edema factor and lethal factor, across the target cell membrane. PA associated with LF causes death when injected, PA associated with EF produces edema. PA induces immunity to infection with anthrax. | [[http://www.uniprot.org/uniprot/PAG_BACAN PAG_BACAN]] One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. PA binds to a receptor (ATR) in sensitive eukaryotic cells, thereby facilitating the translocation of the enzymatic toxin components, edema factor and lethal factor, across the target cell membrane. PA associated with LF causes death when injected, PA associated with EF produces edema. PA induces immunity to infection with anthrax. | ||
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== Publication Abstract from PubMed == | |||
Natural selection shapes protein solubility to physiological requirements and recombinant applications that require higher protein concentrations are often problematic. This raises the question whether the solubility of natural protein sequences can be improved. We here show an anti-correlation between the number of aggregation prone regions (APRs) in a protein sequence and its solubility, suggesting that mutational suppression of APRs provides a simple strategy to increase protein solubility. We show that mutations at specific positions within a protein structure can act as APR suppressors without affecting protein stability. These hot spots for protein solubility are both structure and sequence dependent but can be computationally predicted. We demonstrate this by reducing the aggregation of human alpha-galactosidase and protective antigen of Bacillus anthracis through mutation. Our results indicate that many proteins possess hot spots allowing to adapt protein solubility independently of structure and function. | |||
Structural hot spots for the solubility of globular proteins.,Ganesan A, Siekierska A, Beerten J, Brams M, Van Durme J, De Baets G, Van der Kant R, Gallardo R, Ramakers M, Langenberg T, Wilkinson H, De Smet F, Ulens C, Rousseau F, Schymkowitz J Nat Commun. 2016 Feb 24;7:10816. doi: 10.1038/ncomms10816. PMID:26905391<ref>PMID:26905391</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
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