DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Xu K., Rajashankar KR., Chan YP., Himanen JP., Broder CC., Nikolov DB. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Xu K., Rajashankar KR., Chan YP., Himanen JP., Broder CC., Nikolov DB. DIP original experiment: DIP-113715X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Xu K., Rajashankar KR., Chan YP., Himanen JP., Broder CC., Nikolov DB. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Xu K., Rajashankar KR., Chan YP., Himanen JP., Broder CC., Nikolov DB. DIP original experiment: DIP-113716X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Xu K., Rajashankar KR., Chan YP., Himanen JP., Broder CC., Nikolov DB. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Xu K., Rajashankar KR., Chan YP., Himanen JP., Broder CC., Nikolov DB. DIP original experiment: DIP-113717X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Xu K., Rajashankar KR., Chan YP., Himanen JP., Broder CC., Nikolov DB. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Xu K., Rajashankar KR., Chan YP., Himanen JP., Broder CC., Nikolov DB. DIP original experiment: DIP-113714X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proceedings of the National Academy of Sciences of the United States of America 2008 imex curation Xu K., Rajashankar KR., Chan YP., Himanen JP., Broder CC., Nikolov DB. 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 Xu K., Rajashankar KR., Chan YP., Himanen JP., Broder CC., Nikolov DB. DIP original experiment: DIP-113713X Proceedings of the National Academy of Sciences of the United States of America 2008 IMEx Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. efnb3_mouse Ephrin-B3 Efnb3 protein protein mouse Mus musculus Mouse MGAPHFGPGGVQVGALLLLGFAGLVSGLSLEPVYWNSANKRFQAEGGYVLYPQIGDRLDLLCPRARPPGPHSSPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEYSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVGQSPRGGAVPRKPVSEMPMERDRGAAHSAEPGRDTIPGDPSSNATSRGAEGPLPPPSMPAVAGAAGGMALLLLGVAGAGGAMCWRRRRAKPSESRHPGPGSFGRGGSLGLGGGGGMGPREAEPGELGIALRGGGTADPPFCPHYEKVSGDYGHPVYIVQDGPPQSPPNIYYKV DIP protein O35393 original sequence version: 65 DIP protein O35393 original sequence version: 88 mint May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons 52F3D58FD209A6B8 q4vcp5_nipav G protein protein nipav Nipah virus MPTESKKVRFENTASDKGKNPSKVIKSYYGTMDIKKINEGLLDSKILSAFNTVIALLGSIVIIVMNIMIIQNYTRSTDNQAMIKDALQSIQQQIKGLADKIGTEIGPKVSLIDTSSTITIPANIGLLGSKISQSTASINENVNEKCKFTLPPLKIHECNISCPNPLPFREYKPQTEGVSNLVGLPNNICLQKTSNQILKPKLISYTLPVVGQSGTCITDPLLAMDEGYFAYSHLEKIGSCSRGVSKQRIIGVGEVLDRGDEVPSLFMTNVWTPSNPNTVYHCSAVYNNEFYYVLCAVSVVGDPILNSTYWSGSLMMTRLAVKPKNNGESYNQHQFALRNIEKGKYDKVMPYGPSGIKQGDTLYFPAVGFLVRTEFKYNDSNCPIAECQYSKPENCRLSMGIRPNSHYILRSGLLKYNLSDEENSKIVFIEISDQRLSIGSPSKIYDSLGQPVFYQASFSWDTMIKFGDVQTVNPLVVNWRDNTVISRPGQSQCPRFNKCPEVCWEGVYNDAFLIDRINWISAGVFLDSNQTAENPVFTVFKDNEVLYRAQLASEDTNAQKTITNCFLLKNKIWCISLVEIYDTGDNVIRPKLFAVKIPEQCT DIP protein Q4VCP5 original sequence version: 29 efnb3-g-1 3 6 unspecified role unspecified role unspecified role unspecified role Region 30-170 Region 30-170 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 7 unspecified role unspecified role unspecified role unspecified role Region 171-602 Region 171-602 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction efnb3-g-2 5 6 unspecified role unspecified role unspecified role unspecified role Region 30-170 Region 30-170 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 7 unspecified role unspecified role unspecified role unspecified role Region 171-602 Region 171-602 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction efnb3-g-3 1 6 unspecified role unspecified role unspecified role unspecified role Region 30-170 Region 30-170 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 7 unspecified role unspecified role unspecified role unspecified role Region 171-602 Region 171-602 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction g-efnb3-1 4 6 unspecified role unspecified role prey prey Region 30-170 Region 30-170 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 7 unspecified role unspecified role bait bait Region 171-602 Region 171-602 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Fc-tag Fc-tag fusion protein fusion protein n-term range n-terminal range n-term range n-term range n-terminal range n-term range spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction efnb3-g-4 2 6 unspecified role unspecified role unspecified role unspecified role Region 30-170 Region 30-170 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 7 unspecified role unspecified role unspecified role unspecified role Region 171-602 Region 171-602 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm direct interaction direct interaction