1omq
From Proteopedia
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| - | [[Image:1omq.jpg|left|200px]] | + | [[Image:1omq.jpg|left|200px]] |
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| - | '''Structure of penetratin in bicellar solution''' | + | {{Structure |
| + | |PDB= 1omq |SIZE=350|CAPTION= <scene name='initialview01'>1omq</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Structure of penetratin in bicellar solution''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OMQ is a [ | + | 1OMQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMQ OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and positioning comparison of two variants of penetratin in two different membrane mimicking systems by NMR., Lindberg M, Biverstahl H, Graslund A, Maler L, Eur J Biochem. 2003 Jul;270(14):3055-63. PMID:[http:// | + | Structure and positioning comparison of two variants of penetratin in two different membrane mimicking systems by NMR., Lindberg M, Biverstahl H, Graslund A, Maler L, Eur J Biochem. 2003 Jul;270(14):3055-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12846839 12846839] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Biverstahl, H.]] | [[Category: Biverstahl, H.]] | ||
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[[Category: Maler, L.]] | [[Category: Maler, L.]] | ||
[[Category: alpha helical in the middle]] | [[Category: alpha helical in the middle]] | ||
| - | [[Category: unstructured at the | + | [[Category: unstructured at the terminal]] |
| - | ''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 13:12:52 2008'' |
Revision as of 11:12, 20 March 2008
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Structure of penetratin in bicellar solution
Overview
The Antennapedia homeodomain protein of Drosophila has the ability to penetrate biological membranes and the third helix of this protein, residues 43-58, known as penetratin (RQIKIWFQNRRMKWKK-amide) has the same translocating properties as the entire protein. The variant, RQI KIFFQNRRMKFKK-amide, here called penetratin (W48F,W56F) does not have the same ability. We have determined a solution structure of penetratin and investigated the position of both peptides in negatively charged bicelles. A helical structure is seen for residues Lys46 through Met54. The secondary structure of the variant penetratin(W48F,W56F) in bicelles appears to be very similar. Paramagnetic spin-label studies and analysis of NOEs between penetratin and the phospholipids show that penetratin is located within the bicelle surface. Penetratin (W48F,W56F) is also located inside the phospholipid bicelle, however, with its N-terminus more deeply inserted than that of wild-type penetratin. The subtle differences in the way the two peptides interact with a membrane in an equilibrium situation could be important for their translocating ability. As a comparison we have also investigated the secondary structure of penetratin(W48F,W56F) in SDS micelles and the results show that the structure is very similar in SDS and bicelles. In contrast, penetratin(W48F,W56F) and penetratin appear to be located differently in SDS micelles. This clearly shows the importance of using realistic membrane mimetics for investigating peptide-membrane interactions.
About this Structure
1OMQ is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structure and positioning comparison of two variants of penetratin in two different membrane mimicking systems by NMR., Lindberg M, Biverstahl H, Graslund A, Maler L, Eur J Biochem. 2003 Jul;270(14):3055-63. PMID:12846839
Page seeded by OCA on Thu Mar 20 13:12:52 2008
