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 Quaternary structure of Dioclea grandiflora lectin assessed by equilibrium sedimentation and crystallographic analysis of recombinant mutants. Quaternary structure of Dioclea grandiflora lectin assessed by equilibrium sedimentation and crystallographic analysis of recombinant mutants. FEBS letters 2015 imex curation Zamora-Caballero S., Pérez A., Sanz L., Bravo J., Calvete JJ. jbravo@ibv.csic.es 21-10-2015: 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 Zamora-Caballero S., Pérez A., Sanz L., Bravo J., Calvete JJ. jbravo@ibv.csic.es Accepted 2015-SEP-25 AT 11:31 BST AT 11:31 BST by LUANA FEBS letters 2015 Only protein-protein interactions imex curation imex curation Quaternary structure of Dioclea grandiflora lectin assessed by equilibrium sedimentation and crystallographic analysis of recombinant mutants. Quaternary structure of Dioclea grandiflora lectin assessed by equilibrium sedimentation and crystallographic analysis of recombinant mutants. FEBS letters 2015 imex curation Zamora-Caballero S., Pérez A., Sanz L., Bravo J., Calvete JJ. jbravo@ibv.csic.es 21-10-2015: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Zamora-Caballero S., Pérez A., Sanz L., Bravo J., Calvete JJ. jbravo@ibv.csic.es Accepted 2015-SEP-25 AT 11:31 BST AT 11:31 BST by LUANA FEBS letters 2015 Only protein-protein interactions imex curation imex curation leca_diogr Lectin alpha chain protein protein diogr diogr Mucana ADTIVAVELDSYPNTDIGDPNYPHIGIDIKSIRSKSTARWNMQTGKVGTVHISYNSVAKRLSAVVSYSGSSSTTVSYDVDLNNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKTNSIADENSLHFSFHKFSQNPKDLILQGDAFTDSDGNLELTKVSSSGDPQGNSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDREPADGITFFIANTDTSIPSGSGGRLLGLFPDAN AF27C8A9B138861D 1-67 2 3 unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f1 leca_diogr-1 2 3 unspecified role unspecified role neutral component neutral component purified purified undefined mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:32:16 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'his51gly_his131asn' undefined mutation mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:27:59 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 's51gly_arg60ala' direct interaction direct interaction f1 1-68 1 3 unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f2 f3 t2 crystal structure of a DGL mutant - H51G H131N