Publication Date:
1988-03-11
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ribi, H O -- Ludwig, D S -- Mercer, K L -- Schoolnik, G K -- Kornberg, R D -- AI21144/AI/NIAID NIH HHS/ -- GM07276-12/GM/NIGMS NIH HHS/ -- GM07365/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Mar 11;239(4845):1272-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3344432" target="_blank"〉PubMed〈/a〉
Keywords:
*Cholera Toxin
;
G(M1) Ganglioside
;
*Liposomes
;
Macromolecular Substances
;
Microscopy, Electron
;
Models, Molecular
;
Phosphatidylethanolamines
;
Protein Conformation
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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