2fbu
From Proteopedia
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[[Image:2fbu.gif|left|200px]] | [[Image:2fbu.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_2fbu| PDB=2fbu | SCENE= }} | |
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'''Solution structure of the N-terminal fragment of human LL-37''' | '''Solution structure of the N-terminal fragment of human LL-37''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FBU is a [[Single protein]] structure | + | 2FBU is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FBU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Li, Y.]] | [[Category: Li, Y.]] | ||
[[Category: Wang, G.]] | [[Category: Wang, G.]] | ||
| - | [[Category: | + | [[Category: Aggregation]] |
| - | [[Category: | + | [[Category: Antimicrobial peptide]] |
| - | [[Category: | + | [[Category: Aromatic-aromatic interaction]] |
| - | [[Category: | + | [[Category: Host defense peptide]] |
| - | [[Category: | + | [[Category: Ll-37]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:42:25 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:42, 4 May 2008
Solution structure of the N-terminal fragment of human LL-37
Overview
To understand the structure and activity relationship of human LL-37, a series of peptide fragments was designed. The N-terminal fragment, LL-37(1-12), was not active, while the C-terminal fragment, LL-37(13-37), killed Escherichia coli, as well as drug-sensitive and drug-resistant cancer cells. A 13-residue core antibacterial and anticancer peptide, corresponding to residues 17-29 of LL-37, was identified based on total correlated spectroscopy by trimming nonessential regions (TOCSY-trim). Because LL-37 acts on bacterial membranes, three-dimensional structures of its fragments were determined in micelles by NMR, including structural refinement by natural abundance 15N and 13C chemical shifts. Aromatic-aromatic interactions in the N-terminal fragment were proposed to be essential for LL-37 aggregation. The LL-37 core peptide adopts a similar structure in the micelles of SDS or dioctanoyl phosphatidylglycerol. This structure is retained in the C-terminal fragment LL-37(13-37) and very likely in intact LL-37 based on peptide-aided signal assignments. The higher antibacterial activity of the LL-37 core peptide than aurein 1.2 was attributed to additional cationic residues. To achieve selective membrane targeting, D-amino acids were incorporated into LL-37(17-32). While the D-peptide showed similar antibacterial activity to the L-diastereomer, it lost toxicity to human cells. Structural analysis revealed hydrophobic defects in the new amphipathic structure of the D-peptide, leading to a much shorter retention time on a reversed-phase HPLC column. It is proposed that hydrophobic defects as a result of incoherent hydrophobic packing provide a structural basis for the improvement in cell selectivity of the LL-37 fragment.
About this Structure
2FBU is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Solution structures of human LL-37 fragments and NMR-based identification of a minimal membrane-targeting antimicrobial and anticancer region., Li X, Li Y, Han H, Miller DW, Wang G, J Am Chem Soc. 2006 May 3;128(17):5776-85. PMID:16637646 Page seeded by OCA on Sun May 4 03:42:25 2008
