Conformational dynamics of the bovine mitochondrial ADP/ATP carrier isoform revealed by hydrogen/deuterium exchange coupled to mass spectrometry

0354271 - MBÚ 2011 RIV US eng J - Článek v odborném periodiku
Rey, M. - Man, Petr - Clemencon, B. - Trezeguet, V. - Brandolin, G. - Forest, E. - Pelosi, L.
Conformational dynamics of the bovine mitochondrial ADP/ATP carrier isoform revealed by hydrogen/deuterium exchange coupled to mass spectrometry.
Journal of Biological Chemistry. Roč. 285, č. 45 (2010), s. 34981-34990. ISSN 0021-9258. E-ISSN 1083-351X
Výzkumný záměr: CEZ:AV0Z50200510
Klíčová slova: ADENINE-NUCLEOTIDE CARRIER * ADP ATP CARRIER * PHOSPHOLIPASE A(2)
Kód oboru RIV: CE - Biochemie
Impakt faktor: 5.328, rok: 2010

Paper describes structural changes of the bovine adenine nucleotide transporter (bAncp). bAncp is an integral membrane protein responsible for the transport of ADP and ATP across the mitochondrial membrane. bAncp can be inhibited by various poisons. We focused on the complex with carboxyatractyloside for which the high-resolution structure is known and with bongkrekic acid for which the mechanism of inhibition remains hidden. Using hydrogen/deuterium exchange coupled to mass spectrometry we showed that each inhibitor locks the carrier in a different conformation and thus offers unique view on the carrier function
Trvalý link: http://hdl.handle.net/11104/0193312