UniProt UniProt http://www.uniprot.org Monomer/dimer transition of the caspase-recruitment domain of human Nod1. Monomer/dimer transition of the caspase-recruitment domain of human Nod1. Biochemistry (0006-2960) 2008 imex curation Srimathi T., Robbins SL., Dubas RL., Hasegawa M., Inohara N., Park YC. Apoptosis - Interactions involving proteins with a function related to apoptosis Young.Park@fccc.edu orchard 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 Srimathi T., Robbins SL., Dubas RL., Hasegawa M., Inohara N., Park YC. Apoptosis - Interactions involving proteins with a function related to apoptosis Young.Park@fccc.edu Accepted 2011-APR-05 by ORCHARD Biochemistry (0006-2960) 2008 orchard Only protein-protein interactions imex curation Monomer/dimer transition of the caspase-recruitment domain of human Nod1. Monomer/dimer transition of the caspase-recruitment domain of human Nod1. Biochemistry (0006-2960) 2008 imex curation Srimathi T., Robbins SL., Dubas RL., Hasegawa M., Inohara N., Park YC. Apoptosis - Interactions involving proteins with a function related to apoptosis Young.Park@fccc.edu orchard 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 Srimathi T., Robbins SL., Dubas RL., Hasegawa M., Inohara N., Park YC. Apoptosis - Interactions involving proteins with a function related to apoptosis Young.Park@fccc.edu Accepted 2011-APR-05 by ORCHARD Biochemistry (0006-2960) 2008 orchard Only protein-protein interactions imex curation nod1_human Nucleotide-binding oligomerization domain-containing protein 1 Caspase recruitment domain-containing protein 4 NOD1 CARD4 protein protein human Homo sapiens Human MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSLACLLDHTTGILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLLRFPHVALFTFDGLDELHSDLDLSRVPDSSCPWEPAHPLVLLANLLSGKLLKGASKLLTARTGIEVPRQFLRKKVLLRGFSPSHLRAYARRMFPERALQDRLLSQLEANPNLCSLCSVPLFCWIIFRCFQHFRAAFEGSPQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETLHAGRDTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELGPGGDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMPPAGAATTSCYPPFLPFQCLQGSGPAREDLFKNKDHFQFTNLFLCGLLSKAKQKLLRHLVPAAALRRKRKALWAHLFSSLRGYLKSLPRVQVESFNQVQAMPTFIWMLRCIYETQSQKVGQLAARGICANYLKLTYCNACSADCSALSFVLHHFPKRLALDLDNNNLNDYGVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAKVYEDEKRIICF DIP protein Q9Y239 original sequence version: 140 DIP protein Q9Y239 original sequence version: 99 DIP protein Q9Y239 original sequence version: 105 0A9DF5FC6487E21A nod1-nod1-1 1 3 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind x-ray diffraction x-ray crystallography X-ray x-ray diffraction X-ray certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction 1.9 A 0.266 R-value 0.222 R-free nod1-nod1-2 2 3 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain region required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig 4