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| {{STRUCTURE_1lt3| PDB=1lt3 | SCENE= }} | | {{STRUCTURE_1lt3| PDB=1lt3 | SCENE= }} |
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| '''HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C'''
| | ===HEAT-LABILE ENTEROTOXIN DOUBLE MUTANT N40C/G166C=== |
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| ==Overview==
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| Cholera toxin (CT) produced by Vibrio cholerae and heat-labile enterotoxin (LT-I), produced by enterotoxigenic Escherichia coli, are AB5 heterohexamers with an ADP-ribosylating A subunit and a GM1 receptor binding B pentamer. These toxins are among the most potent mucosal adjuvants known and, hence, are of interest both for the development of anti-diarrheal vaccines against cholera or enterotoxigenic Escherichia coli diarrhea and also for vaccines in general. However, the A subunits of CT and LT-I are known to be relatively temperature sensitive. To improve the thermostability of LT-I an additional disulfide bond was introduced in the A1 subunit by means of the double mutation N40C and G166C. The crystal structure of this double mutant of LT-I has been determined to 2.0 A resolution. The protein structure of the N40C/G166C double mutant is very similar to the native structure except for a few local shifts near the new disulfide bond. The introduction of this additional disulfide bond increases the thermal stability of the A subunit of LT-I by 6 degrees C. The enhancement in thermostability could make this disulfide bond variant of LT-I of considerable interest for the design of enterotoxin-based vaccines.
| | The line below this paragraph, {{ABSTRACT_PUBMED_9416616}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9416616 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9416616}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Enterotoxin]] | | [[Category: Enterotoxin]] |
| [[Category: Signal]] | | [[Category: Signal]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:15:39 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:07:43 2008'' |
