Dépôt numérique

Structural and functional comparison of two human homologues of the RNase A superfamily

Gagnon, Jacinthe, Sarvan, Sabina, Gagné, Donald, Couture, Jean-François et Doucet, Nicolas . Structural and functional comparison of two human homologues of the RNase A superfamily In: 2nd Protein Engineering Canada Conference (PEC), 17-19 Juin 2016, Ottawa, Canada.

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Members of the ribonuclease (RNase) A superfamily have been ass ociated with a great variety of biological functions, in addition to their strictly conserved r ibonucleolytic activities. For example, some RNases have antibacterial, cytotoxic, angiogenic, immunosu ppressive, antitumoral and antiviral properties. In humans, there are 8 members of the RNa se A superfamily. These enzymes have rapidly evolved and possess various degrees of homology an d enzymatic activity. The first crystal structure of RNase 6 (or RNase k6) has been only recent ly resolved in presence of sulfate anions that bind at two distinct sites on the enzyme. We have c rystallized RNase 6 in presence of phosphate anions, thus also demonstrating two distinct binding sites with phosphate. One of these sites is located in loop 4 and has never been identified in any other member of the human RNases. The biophysical properties of the RNases A, 4 and 6 were also a nalyzed by nuclear magnetic resonance (NMR) titration and by isothermal calorimetric titrat ion (ITC) with two ligands: 3 ́-UMP and 5 ́-AMP. The similarities and differences between these anal yses will be presented. The crystal structure of RNase 6 will also be compared with those o f RNase A and RNase 4. Finally, the structural differences that may partially explain their fun ctional identity will be discussed, therefore offering many essential clues towards the understandi ng of their biological functions.

Type de document: Document issu d'une conférence ou d'un atelier
Mots-clés libres: -
Centre: Centre INRS-Institut Armand Frappier
Date de dépôt: 25 juin 2018 15:57
Dernière modification: 25 juin 2018 15:57
URI: https://espace.inrs.ca/id/eprint/5787

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