IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Purification, crystallization and preliminary data analysis of the ligand-receptor complex of the growth and differentiation factor 5 variant R57A (GDF5R57A) and BMP receptor IA (BRIA). Purification, crystallization and preliminary data analysis of the ligand-receptor complex of the growth and differentiation factor 5 variant R57A (GDF5R57A) and BMP receptor IA (BRIA). Acta crystallographica. Section F, Structural biology and crystallization communications 2011 imex curation Nickel J., Kotzsch A., Sebald W., Mueller TD. Rare diseases - Interactions investigated in the context of Rare genetic disease mueller@biozentrum.uni-wuerzburg.de 04-05-20: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Nickel J., Kotzsch A., Sebald W., Mueller TD. Rare diseases - Interactions investigated in the context of Rare genetic disease The position of mutation, according to authors is 57-Arg; however the construct range used is 381-501 and Arg-57 is not possible within the range. So the mutation was mapped to 57th Arg from 381st amino acid mueller@biozentrum.uni-wuerzburg.de Accepted 2020-JAN-16 AT 10:55 GMT AT 10:55 GMT by ORCHARD Acta crystallographica. Section F, Structural biology and crystallization communications 2011 Only protein-protein interactions imex curation imex curation bmr1a_human Bone morphogenetic protein receptor type-1A ACVRLK3 ALK3 BMPR1A Serine/threonine-protein kinase receptor R5 Activin receptor-like kinase 3 protein protein human Homo sapiens Human MPQLYIYIRLLGAYLFIISRVQGQNLDSMLHGTGMKSDSDQKKSENGVTLAPEDTLPFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQPTLPPVVIGPFFDGSIRWLVLLISMAVCIIAMIIFSSCFCYKHYCKSISSRRRYNRDLEQDEAFIPVGESLKDLIDQSQSSGSGSGLPLLVQRTIAKQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVKRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVESQDVKI DIP protein P36894 original sequence version: 180 DIP protein P36894 original sequence version: 179 DIP protein P36894 original sequence version: 185 00CE2DDDA3A44170 gdf5_human Growth/differentiation factor 5 GDF5 CDMP1 Cartilage-derived morphogenetic protein 1 Radotermin BMP14 Bone morphogenetic protein 14 Lipopolysaccharide-associated protein 4 protein protein human Homo sapiens Human MRLPKLLTFLLWYLAWLDLEFICTVLGAPDLGQRPQGTRPGLAKAEAKERPPLARNVFRPGGHSYGGGATNANARAKGGTGQTGGLTQPKKDEPKKLPPRPGGPEPKPGHPPQTRQATARTVTPKGQLPGGKAPPKAGSVPSSFLLKKAREPGPPREPKEPFRPPPITPHEYMLSLYRTLSDADRKGGNSSVKLEAGLANTITSFIDKGQDDRGPVVRKQRYVFDISALEKDGLLGAELRILRKKPSDTAKPAAPGGGRAAQLKLSSCPSGRQPASLLDVRSVPGLDGSGWEVFDIWKLFRNFKNSAQLCLELEAWERGRAVDLRGLGFDRAARQVHEKALFLVFGRTKKRDLFFNEIKARSGQDDKTVYEYLFSQRRKRRAPLATRQGKRPSKNLKARCSRKALHVNFKDMGWDDWIIAPLEYEAFHCEGLCEFPLRSHLEPTNHAVIQTLMNSMDPESTPPTCCVPTRLSPISILFIDSANNVVYKQYEDMVVESCGCR mint 37985F2D15C4F5EF bmpr1a-gdf5-3 1 3 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P43026:p.Arg438Ala mutation mutation certain certain sequence position certain certain certain sequence position certain R A Tue Jun 30 18:34:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg438Ala' ecoli Escherichia coli (strain K12) 2 unspecified role unspecified role neutral component neutral component purified purified extracellular domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Table 1