DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus. Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Acharya R., Carnevale V., Fiorin G., Levine BG., Polishchuk AL., Balannik V., Samish I., Lamb RA., Pinto LH., DeGrado WF., Klein ML. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Acharya R., Carnevale V., Fiorin G., Levine BG., Polishchuk AL., Balannik V., Samish I., Lamb RA., Pinto LH., DeGrado WF., Klein ML. DIP original experiment: DIP-219933X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Structure and mechanism of proton transport through the transmembrane tetrameric M2 protein bundle of the influenza A virus. m2_i72a2 Matrix protein 2 M Proton channel protein M2 protein protein i72a2 Influenza A virus (strain A/Udorn/307/1972 H3N2) MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRFFEHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVSIELE DIP protein P63231 original sequence version: 60 3CDD4DE90D7B16A4 m-5 1 2 unspecified role unspecified role unspecified role unspecified role Transmembrane domain Region 25-46 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction