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 Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients. Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients. EMBO J. (0261-4189) 2010 imex curation Kenniston JA., Lemmon MA. Only protein-protein interactions in vitro In vitro saxs x ray scattering saxs predetermined predetermined participant predetermined Kenniston JA., Lemmon MA. EMBO J. (0261-4189) 2010 Only protein-protein interactions imex curation Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients. Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients. EMBO J. (0261-4189) 2010 imex curation Kenniston JA., Lemmon MA. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Kenniston JA., Lemmon MA. EMBO J. (0261-4189) 2010 Only protein-protein interactions imex curation dyn1_human Dynamin-1 DNM1 DNM protein protein human Homo sapiens Human MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVEEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL DIP protein Q05193 original sequence version: 142 DIP protein Q05193 original sequence version: 113 DIP protein Q05193 original sequence version: 100 DIP protein Q05193 original sequence version: 115 DIP protein Q05193-1 original sequence version: 111 DIP protein Q05193 original sequence version: 153 7FCD8CB572FFEAEF dnm1-3 2 Dynamin 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction sf3 mint We also deleted the unstructured C-terminal PRD domain that is reported to enhance self-assembly (Warnock et al, 1997). The resulting construct yielded protein that is extremely soluble (to X400 mM) compared with wild-type dynamin, and behaves as a monodisperse dimer in sedimentation velocity ultracentrifugation experiments (Supplementary Figure S3). dnm1-3 1 Dynamin 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction mint Parameters derived from the SAXS scattering curves (Figure 6A) revealed a strong similarity in overall solution behaviour of wild-type dimeric dynamin and these two CNM variants (Supplementary Table SI). f6 st1 sf5