| Autor: |
MERRITT, EA, SIXMA, TK, KALK, KH, VANZANTEN, BAM, HOL, WGJ |
| Přispěvatelé: |
Groningen Biomolecular Sciences and Biotechnology |
| Jazyk: |
angličtina |
| Rok vydání: |
1994 |
| Předmět: |
|
| Zdroj: |
Molecular Microbiology, 13(4), 745-753. Wiley |
| ISSN: |
0950-382X |
| Popis: |
The galactose-binding site in cholera toxin and the closely related heat-labile enterotoxin (LT) from Escherichia coil is an attractive target for the rational design of potential anti-cholera drugs. In this paper we analyse the molecular structure of this binding site as seen in several crystal structures, including that of an LT:galactose complex which we report here at 2.2 Angstrom resolution. The binding surface on the free toxin contains several tightly associated water molecules and a relatively flexible loop consisting of residues 51-60 of the B subunit. During receptor binding this loop becomes tightly ordered by forming hydrogen bonds jointly to the G(M1) pentasaccharide and to a set of water molecules which stabilize the toxin:receptor complex. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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