7AL0

Crystal Structure of Heymonin, a Novel Frog-derived Peptide

Summary for 7AL0

• Entry DOI: 10.2210/pdb7al0/pdb
• Descriptor: Heymonin, CHLORIDE ION (3 entities in total)
• Functional Keywords: antimicrobial peptide, inflammation, microhyla heymonsivogt, antimicrobial protein
• Biological source: Microhyla heymonsi
• Total number of polymer chains: 1
• Total formula weight: 4341.30

Authors

Kascakova, B.,Prudnikova, T.,Kuta Smatanova, I.,Xu, X. (deposition date: 2020-10-03, release date: 2021-04-21, Last modification date: 2024-10-23)

Primary citation

Chai, J.,Chen, X.,Ye, T.,Zeng, B.,Zeng, Q.,Wu, J.,Kascakova, B.,Martins, L.A.,Prudnikova, T.,Smatanova, I.K.,Kotsyfakis, M.,Xu, X.
Characterization and functional analysis of cathelicidin-MH, a novel frog-derived peptide with anti-septicemic properties.
Elife, 10:-, 2021

PubMed Abstract: Antimicrobial peptides form part of the innate immune response and play a vital role in host defense against pathogens. Here we report a new antimicrobial peptide belonging to the cathelicidin family, cathelicidin-MH (cath-MH), from the skin of frog. Cath-MH has a single α-helical structure in membrane-mimetic environments and is antimicrobial against fungi and bacteria, especially Gram-negative bacteria. In contrast to other cathelicidins, cath-MH suppresses coagulation by affecting the enzymatic activities of tissue plasminogen activator, plasmin, β-tryptase, elastase, thrombin, and chymase. Cath-MH protects against lipopolysaccharide (LPS)- and cecal ligation and puncture-induced sepsis, effectively ameliorating multiorgan pathology and inflammatory cytokine through its antimicrobial, LPS-neutralizing, coagulation suppressing effects as well as suppression of MAPK signaling. Taken together, these data suggest that cath-MH is an attractive candidate therapeutic agent for the treatment of septic shock.

PubMed: 33875135
DOI: 10.7554/eLife.64411

Experimental method

X-RAY DIFFRACTION (2.2 Å)