1SMZ
Structure of Transportan in phospholipid bicellar solution
Summary for 1SMZ
Entry DOI | 10.2210/pdb1smz/pdb |
NMR Information | BMRB: 6151 |
Descriptor | Transportan in bicellar solution with [DMPC]/[DHPC]=0.33 (1 entity in total) |
Functional Keywords | transport protein |
Total number of polymer chains | 1 |
Total formula weight | 2845.47 |
Authors | Barany-Wallje, E.,Andersson, A.,Maler, L.,Graslund, A. (deposition date: 2004-03-10, release date: 2004-03-16, Last modification date: 2024-05-22) |
Primary citation | Andersson, A. NMR solution structure and position of transportan in neutral phospholipid bicelles Febs Lett., 567:265-269, 2004 Cited by PubMed Abstract: Transportan is a chimeric cell-penetrating peptide constructed from the peptides galanin and mastoparan, which has the ability to internalize living cells carrying a hydrophilic load. In this study, we have determined the NMR solution structure and investigated the position of transportan in neutral bicelles. The structure revealed a well-defined alpha-helix in the C-terminal mastoparan part of the peptide and a weaker tendency to form an alpha-helix in the N-terminal domain. The position of the peptide in relation to the membrane, as studied by adding paramagnetic probes, shows that the peptide lies parallel to, and in the head-group region of the membrane surface. This result is supported by amide proton secondary chemical shifts. PubMed: 15178334DOI: 10.1016/j.febslet.2004.04.079 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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