Citation

Coronado MA, Ullah A, da Silva LS, Chaves-Moreira D, Vuitika L, Chaim OM, Veiga SS, Chahine J, Murakami MT, Arni RK. Curr. Protein Pept. Sci. 2015; 16(8): 768-774.

Affiliation

Centro Multiusuario de Inovacao Biomolecular, Departamento de Fisica, Universidade Estadual Paulista (UNESP), Sao Jose do Rio Preto, 15054-000 SP, Brazil. arni@sjrp.unesp.br.

Copyright

(Copyright © 2015, Bentham Science Publishers)

DOI

unavailable

PMID

25961401

Abstract

Phospholipases D (PLDs) the major dermonecrotic factors from brown spider venoms trigger a range of biological reactions both in vitro and in vivo. Despite their clinical relevance in loxoscelism, structural data is restricted to the apo-form of these enzymes, which has been instrumental in understanding the functional differences between the class I and II spider PLDs. The crystal structures of the native class II PLD from Loxosceles intermedia complexed with myo-inositol 1-phosphate and the inactive mutant H12A complexed with fatty acids indicate the existence of a strong ligand-dependent conformation change of the highly conserved aromatic residues, Tyr 223 and Trp225 indicating their roles in substrate binding. These results provided insights into the structural determinants for substrate recognition and binding by class II PLDs.

Language: en