From Proteopedia
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| - | [[Image:1hr1.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1hr1| PDB=1hr1 | SCENE= }} | | {{STRUCTURE_1hr1| PDB=1hr1 | SCENE= }} |
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| - | '''STRUCTURE OF AN INDOLICIDIN PEPTIDE DERIVATIVE WITH P-->A SUBSTITUTION'''
| + | ===STRUCTURE OF AN INDOLICIDIN PEPTIDE DERIVATIVE WITH P-->A SUBSTITUTION=== |
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| - | ==Overview==
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| - | Indolicidin, an antimicrobial peptide with a unique amino acid sequence (ILPWKWPWWPWRR-NH(2)) is found in bovine neutrophils. A derivative of indolicidin, CP10A, has alanine residues substituted for proline residues and has improved activity against Gram-positive organisms. Transmission electron microscopy of Staphylococcus aureus and Staphylococcus epidermidis treated with CP10A showed mesosome-like structures in the cytoplasm. The peptide at 2-fold the minimal inhibitory concentration did not show significant killing of S. aureus ISP67 (a histidine, uridine, and thymidine auxotroph) but did show an early effect on histidine and uridine incorporation and, later, an effect on thymidine incorporation. Upon interaction with liposomes, detergents, and lipoteichoic acid, CP10A was shown by circular dichroism spectroscopy to undergo a change in secondary structure. Fluorescence spectroscopy indicated that the tryptophan residues were located at the hydrophobic/hydrophilic interface of liposomes and detergent micelles and were inaccessible to the aqueous quencher KI. The three-dimensional structure of CP10A in the lipid mimetic dodecylphosphocholine was determined using two-dimensional NMR methods and was characterized as a short, amphipathic helical structure, whereas indolicidin was previously shown to have an extended structure. These studies have introduced a cationic peptide with a unique structure and an ability to interact with membranes and to affect intracellular synthesis of proteins, RNA, and DNA.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11294848}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11294848 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11294848}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1HR1 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HR1 OCA]. | + | 1HR1 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HR1 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Rozek, A.]] | | [[Category: Rozek, A.]] |
| | [[Category: Alpha-helix,cationic antimicrobial peptide]] | | [[Category: Alpha-helix,cationic antimicrobial peptide]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:08:49 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:34:13 2008'' |
Revision as of 05:34, 1 July 2008
Template:STRUCTURE 1hr1
STRUCTURE OF AN INDOLICIDIN PEPTIDE DERIVATIVE WITH P-->A SUBSTITUTION
Template:ABSTRACT PUBMED 11294848
About this Structure
1HR1 is a Single protein structure. Full experimental information is available from OCA.
Reference
Structure and mechanism of action of an indolicidin peptide derivative with improved activity against gram-positive bacteria., Friedrich CL, Rozek A, Patrzykat A, Hancock RE, J Biol Chem. 2001 Jun 29;276(26):24015-22. Epub 2001 Apr 9. PMID:11294848
Page seeded by OCA on Tue Jul 1 08:34:13 2008
