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 http://mint.bio.uniroma2.it/mint anonymous-2013q-1 A S52P Mutation in the “α-crystallin domain" of Mycobacterium leprae HSP18 Reduces its Oligomeric Size and Chaperone Function in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Nandi S.K., Rehna E.A., Panda A.K., Shiburaj S., Dharmalingam K., Biswas A. abiswas@iitbbs.ac.in FEBS J. (1742-464X) 2013 Only protein-protein interactions imex curation 18kd_mycle 18 kDa antigen hsp18 HSP 16.7 ML1795 protein protein mycle Mycobacterium leprae (strain TN) MLMRTDPFRELDRFAEQVLGTSARPAVMPMDAWREGEEFVVEFDLPGIKADSLDIDIERNVVTVRAERPGVDPDREMLAAERPRGVFNRQLVLGENLDTERILASYQEGVLKLSIPVAERAKPRKISVDRGNNGHQTINKTAHEIIDA hsp18-hsp18 1437270 n/a HSP18 1437271 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag predetermined featur predetermined feature predetermined featur undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false P12809:p.Ser52Pro mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) n/a HSP18 1437271 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P12809:p.Ser52Pro mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false his-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag predetermined featur predetermined feature predetermined featur undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false ecoli Escherichia coli (strain K12) direct interaction direct interaction false false false f9 Together, these data suggest that subtle changes in secondary and in the tertiary structure caused by S52P mutation in the ACD of HSP18 led to a decrease in the average oligomeric size, consisting of ~29 subunits in the wild type protein to ~9 subunits in the mutant protein.