| Autor: |
Ribi HO; Department of Cell Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, CA 94305., Ludwig DS, Mercer KL, Schoolnik GK, Kornberg RD |
| Jazyk: |
angličtina |
| Zdroj: |
Science (New York, N.Y.) [Science] 1988 Mar 11; Vol. 239 (4845), pp. 1272-6. |
| DOI: |
10.1126/science.3344432 |
| Abstrakt: |
Two-dimensional crystals of cholera toxin bound to receptors in a lipid membrane give diffraction extending to 15 A resolution. Three-dimensional structure determination reveals a ring of five B subunits on the membrane surface, with one-third of the A subunit occupying the center of the ring. The remaining mass of the A subunit appears to penetrate the hydrophobic interior of the membrane. Cleavage of a disulfide bond in the A subunit, which activates the toxin, causes a major conformational change, with the A subunit mostly exiting from the B ring. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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