Dynamin-type guanine nucleotide-binding (G) domain
IPR030381
Definition
This entry represents the dynamin-type guanine nucleotide-binding (G) domain. Dynamin superfamily members are large GTPases, conserved throughout evolution, that function primarily as mechanochemical enzymes involved in membrane scission events [[cite:PMID:15004222], [cite:PMID:16403025]]. Dynamin itself is a microtubule-associated force-producing protein of approximately 100 kDa, critical for endocytic membrane fission and membrane remodelling PMID:22233676. All members share a common architecture comprising an N-terminal GTPase domain (see [interpro:IPR001401]), followed by a middle (stalk) domain, and a C-terminal coiled-coil GTPase effector domain (GED). The middle domain dimerises in a cross-like fashion, forming a dynamin dimer in which the two GTPase domains are oriented in opposite directions PMID:22233676. The GED is largely α-helical in nature and mediates higher-order assembly through intermolecular packing of helices; it also functions as a GTPase-activating protein (GAP) for dynamin's intrinsic GTPase activity PMID:16403025. The superfamily is subdivided into several subgroups based on domain organisation: classical dynamins, dynamin-like proteins (Dlps), Mx proteins, optic atrophy 1 protein (OPA1), mitofusins, guanylate-binding proteins (GBPs), and atlastins. Most members contain additional domains that characterise the different subgroups. For example, classical dynamins contain a lipid-binding pleckstrin homology (PH) domain (see [interpro:IPR001849]) between the middle domain and the GED, as well as a C-terminal proline-arginine-rich domain (PRD) that interacts with numerous SH3 domain-containing binding partners. Dlps lack the PRD but possess a PH domain, which may be highly divergent. These various domains confer a range of biochemical properties and cellular localisations, explaining the diverse biological roles of dynamin superfamily members in endocytosis, intracellular trafficking, organelle fission and fusion, cytokinesis, and pathogen resistance [[cite:PMID:15004222], [cite:PMID:16403025], [cite:PMID:16938290], [cite:PMID:17533148]].
14 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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