1smz
From Proteopedia
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| - | [[Image:1smz.gif|left|200px]] | + | [[Image:1smz.gif|left|200px]] |
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| - | '''Structure of Transportan in phospholipid bicellar solution''' | + | {{Structure |
| + | |PDB= 1smz |SIZE=350|CAPTION= <scene name='initialview01'>1smz</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of Transportan in phospholipid bicellar solution''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SMZ is a [ | + | 1SMZ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMZ OCA]. |
==Reference== | ==Reference== | ||
| - | NMR solution structure and position of transportan in neutral phospholipid bicelles., Barany-Wallje E, Andersson A, Graslund A, Maler L, FEBS Lett. 2004 Jun 4;567(2-3):265-9. PMID:[http:// | + | NMR solution structure and position of transportan in neutral phospholipid bicelles., Barany-Wallje E, Andersson A, Graslund A, Maler L, FEBS Lett. 2004 Jun 4;567(2-3):265-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15178334 15178334] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Andersson, A.]] | [[Category: Andersson, A.]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:07:04 2008'' |
Revision as of 12:07, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of Transportan in phospholipid bicellar solution
Overview
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.
About this Structure
1SMZ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
NMR solution structure and position of transportan in neutral phospholipid bicelles., Barany-Wallje E, Andersson A, Graslund A, Maler L, FEBS Lett. 2004 Jun 4;567(2-3):265-9. PMID:15178334
Page seeded by OCA on Thu Mar 20 14:07:04 2008
