Structure and topology of diphtheria toxin R domain in lipid membranes
The interaction of the receptor-binding domain (R domain) of diphtheria toxin with a pure lipid membrane has been characterized by several approaches. Using a photoactivatable lipid, the R domain has been shown to deeply insert in the lipid membrane. Three regions of the R domain (residues 380-421, 422-441, and 442 to about 483) are protected by their interaction with the membrane from externally added proteases. At least one of these regions is deeply interacting with the lipid membrane, as evidenced by the location of Cys 461 and 471 determined by fluorescence experiments. Binding of the R domain to the lipid membrane is characterized by the appearance of an alpha-helical component whose orientation is compatible with a transmembrane orientation.
| Medienart: |
Artikel |
|---|
| Erscheinungsjahr: |
1999 |
|---|---|
| Erschienen: |
1999 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:38 |
|---|---|
| Enthalten in: |
Biochemistry - 38(1999), 2 vom: 12. Jan., Seite 660-6 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Quertenmont, P [VerfasserIn] |
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| Anmerkungen: |
Date Completed 16.02.1999 Date Revised 20.11.2014 published: Print Citation Status MEDLINE |
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| Förderinstitution / Projekttitel: |
|
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| PPN (Katalog-ID): |
NLM098240595 |
|---|
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| 041 | |a eng | ||
| 100 | 1 | |a Quertenmont, P |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Structure and topology of diphtheria toxin R domain in lipid membranes |
| 264 | 1 | |c 1999 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
| 338 | |a Band |b nc |2 rdacarrier | ||
| 500 | |a Date Completed 16.02.1999 | ||
| 500 | |a Date Revised 20.11.2014 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a The interaction of the receptor-binding domain (R domain) of diphtheria toxin with a pure lipid membrane has been characterized by several approaches. Using a photoactivatable lipid, the R domain has been shown to deeply insert in the lipid membrane. Three regions of the R domain (residues 380-421, 422-441, and 442 to about 483) are protected by their interaction with the membrane from externally added proteases. At least one of these regions is deeply interacting with the lipid membrane, as evidenced by the location of Cys 461 and 471 determined by fluorescence experiments. Binding of the R domain to the lipid membrane is characterized by the appearance of an alpha-helical component whose orientation is compatible with a transmembrane orientation | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 7 | |a Diphtheria Toxin |2 NLM | |
| 650 | 7 | |a Heparin-binding EGF-like Growth Factor |2 NLM | |
| 650 | 7 | |a Intercellular Signaling Peptides and Proteins |2 NLM | |
| 650 | 7 | |a Liposomes |2 NLM | |
| 650 | 7 | |a Membrane Lipids |2 NLM | |
| 650 | 7 | |a Peptide Fragments |2 NLM | |
| 650 | 7 | |a Proteolipids |2 NLM | |
| 650 | 7 | |a Receptors, Cell Surface |2 NLM | |
| 650 | 7 | |a proteoliposomes |2 NLM | |
| 650 | 7 | |a Tryptophan |2 NLM | |
| 650 | 7 | |a 8DUH1N11BX |2 NLM | |
| 700 | 1 | |a Wolff, C |e verfasserin |4 aut | |
| 700 | 1 | |a Wattiez, R |e verfasserin |4 aut | |
| 700 | 1 | |a Vander Borght, P |e verfasserin |4 aut | |
| 700 | 1 | |a Falmagne, P |e verfasserin |4 aut | |
| 700 | 1 | |a Ruysschaert, J M |e verfasserin |4 aut | |
| 700 | 1 | |a Cabiaux, V |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Biochemistry |d 1962 |g 38(1999), 2 vom: 12. Jan., Seite 660-6 |w (DE-627)NLM000000469 |x 1520-4995 |7 nnns |
| 773 | 1 | 8 | |g volume:38 |g year:1999 |g number:2 |g day:12 |g month:01 |g pages:660-6 |
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| 952 | |d 38 |j 1999 |e 2 |b 12 |c 01 |h 660-6 | ||