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PDBsum entry 2m2c
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References listed in PDB file
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Key reference
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Title
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Indolicidin targets duplex DNA: structural and mechanistic insight through a combination of spectroscopy and microscopy.
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Authors
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A.Ghosh,
R.K.Kar,
J.Jana,
A.Saha,
B.Jana,
J.Krishnamoorthy,
D.Kumar,
S.Ghosh,
S.Chatterjee,
A.Bhunia.
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Ref.
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Chemmedchem, 2014,
9,
2052-2058.
[DOI no: ]
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PubMed id
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Abstract
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Indolicidin (IR13), a 13-residue antimicrobial peptide from the cathelicidin
family, is known to exhibit a broad spectrum of antimicrobial activity against
various microorganisms. This peptide inhibits bacterial DNA synthesis resulting
in cell filamentation. However, the precise mechanism remains unclear and
requires further investigation. The central PWWP motif of IR13 provides a unique
structural element that can wrap around, and thus stabilize, duplex B-type DNA
structures. Replacements of the central Trp-Trp pair with Ala-Ala, His-His, or
Phe-Phe residues in the PxxP motif significantly affects the ability of the
peptide to stabilize duplex DNA. Results of microscopy studies in conjunction
with spectroscopic data confirm that the DNA duplex is stabilized by IR13,
thereby inhibiting DNA replication and transcription. In this study we provide
high-resolution structural information on the interaction between indolicidin
and DNA, which will be beneficial for the design of novel therapeutic
antibiotics based on peptide scaffolds.
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Headers
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