Product Description
Original Source data:
Structure of partially-activated E. coli heat-labile enterotoxin (LT) at 2.6 A resolution.
Merritt, E.A., Pronk, S.E., Sixma, T.K., Kalk, K.H., van Zanten, B.A., Hol, W.G.
Journal: (1994) FEBS Lett. 337: 88-92
PubMed: 8276119
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PubMed Abstract:
Biological toxicity of E. coli heat-labile enterotoxin and the closely related cholera toxin requires that the assembled toxin be activated by proteolytic cleavage of the A subunit and reduction of a disulfide bond internal to the A subunit. The structural... [ Read More & Search PubMed Abstracts ]