MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it The guanine cap of human guanylate-binding protein 1 is responsible for dimerization and self-activation of GTP hydrolysis. The guanine cap of human guanylate-binding protein 1 is responsible for dimerization and self-activation of GTP hydrolysis. FEBS J. (1742-464X) 2012 imex curation Wehner M., Kunzelmann S., Herrmann C. 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 Wehner M., Kunzelmann S., Herrmann C. FEBS J. (1742-464X) 2012 Only protein-protein interactions imex curation gbp1_human Guanylate-binding protein 1 GBP1 GTP-binding protein 1 Guanine nucleotide-binding protein 1 Interferon-induced guanylate-binding protein 1 protein protein human Homo sapiens Human MASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTETLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSALLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS DIP protein P32455 original sequence version: 122 3A06741218360732 gbp1 1 hGBP1 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P32455:p.Arg240Ala mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R A Tue Jul 12 10:05:35 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 16:05:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg240ala' Tue Jun 30 17:50:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg240Ala' Stoichiometry: 2.0 direct interaction direct interaction mint In the case of wild-type hGBP1 the first dimerization at the LG domains occurs as a result of GTP-binding f3 t2 st2 sf3 To directly analyze the oligomerization behaviour of the mutants, we performed analytical gel filtration experiments. In agreement with the hydrolysis data we observed that mutants with strongly increased Kdimer do not or only partly form dimers in presence of GppNHp (figure 3, supplementary figure S3, and table 2)Using a protein concentration (20 μM) that saturates dimer formation of wild-type hGBP1, no sign of dimer formation was observed with the mutant R240A. The mutations R244A, R245A and D259A showed increasing fractions of a dimeric species, but more than 90% of the protein was in a monomer state. D192A and E105A exhibit very similar behaviour to the wildtype protein. All mutants that showed only minor effects on self-activated hydrolysis and dimerization were also able to form tetramers in complex with GDP aluminum fluoride similar to wildtype (table 2 and supplementary table S2).