%0 Journal Article %1 WOS:000390513800006 %A de Sousa, Bruno Lopes %A Nagano, Celso Shiniti %A da Simoes, Rafael Conceicao %A Silva-Filho, Jose Caetano %A da Silva Cunha, Rodrigo Maranguape %A Cajazeiras, Joao Batista %A do Nascimento, Kyria Santiago %A Cavada, Benildo Sousa %C 65 RUE CAMILLE DESMOULINS, CS50083, 92442 ISSY-LES-MOULINEAUX, FRANCE %D 2016 %I ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER %J BIOCHIMIE %K Diocleinae; Functional Precursor; Structure analysis} prediction; {Lectin; %P 54-67 %R 10.1016/j.biochi.2016.09.010 %T Structure prediction and functional analysis of a non-permutated lectin from Dioclea grandiflora %V 131 %X Legume lectins have been widely studied and applied for many purposes in the last few decades, but many of their physiological aspects remain elusive. The Diocleinae legume subtribe, which includes intensively explored lectins, such as ConA, presents an unusual and extensive post-translational process which results in minor alterations in protein structure, in turn making its function elusive. Despite previous reports about Diocleinae precursor activity, no structural or functional analyses have ever been carried out to understand the impacts of post-translational processing relative to lectin structure and binding specificity. Here we analyzed the functionality of a non glycosylated, recombinantly expressed lectin precursor from Dioclea grandiflora through inhibition assays, corroborating the experimental data with structural information generated by molecular modeling, docking calculations and molecular dynamics simulations. We demonstrate that Diocleinae precursors are active and share the same carbohydrate specificity as mature lectins. At the same time, however, subtle structural alterations were detected and mostly result in an ``incomplete'' functionality of the precursor, as consequence of an immature binding site and an unstructured tetramer interface, affecting carbohydrate binding and oligomer formation, respectively. (C) 2016 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.

@article{WOS:000390513800006, abstract = {Legume lectins have been widely studied and applied for many purposes in the last few decades, but many of their physiological aspects remain elusive. The Diocleinae legume subtribe, which includes intensively explored lectins, such as ConA, presents an unusual and extensive post-translational process which results in minor alterations in protein structure, in turn making its function elusive. Despite previous reports about Diocleinae precursor activity, no structural or functional analyses have ever been carried out to understand the impacts of post-translational processing relative to lectin structure and binding specificity. Here we analyzed the functionality of a non glycosylated, recombinantly expressed lectin precursor from Dioclea grandiflora through inhibition assays, corroborating the experimental data with structural information generated by molecular modeling, docking calculations and molecular dynamics simulations. We demonstrate that Diocleinae precursors are active and share the same carbohydrate specificity as mature lectins. At the same time, however, subtle structural alterations were detected and mostly result in an ``incomplete'' functionality of the precursor, as consequence of an immature binding site and an unstructured tetramer interface, affecting carbohydrate binding and oligomer formation, respectively. (C) 2016 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.}, added-at = {2022-05-23T20:00:14.000+0200}, address = {65 RUE CAMILLE DESMOULINS, CS50083, 92442 ISSY-LES-MOULINEAUX, FRANCE}, author = {de Sousa, Bruno Lopes and Nagano, Celso Shiniti and da Simoes, Rafael Conceicao and Silva-Filho, Jose Caetano and da Silva Cunha, Rodrigo Maranguape and Cajazeiras, Joao Batista and do Nascimento, Kyria Santiago and Cavada, Benildo Sousa}, biburl = {https://www.bibsonomy.org/bibtex/2c02e32ebe472dc78c3870e5837acbc01/ppgfis_ufc_br}, doi = {10.1016/j.biochi.2016.09.010}, interhash = {4f0f620f87afad3ba17ad638c7aefdce}, intrahash = {c02e32ebe472dc78c3870e5837acbc01}, issn = {0300-9084}, journal = {BIOCHIMIE}, keywords = {Diocleinae; Functional Precursor; Structure analysis} prediction; {Lectin;}, pages = {54-67}, publisher = {ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER}, pubstate = {published}, timestamp = {2022-05-23T20:00:14.000+0200}, title = {Structure prediction and functional analysis of a non-permutated lectin from Dioclea grandiflora}, tppubtype = {article}, volume = 131, year = 2016 }