Proposed model of interaction of Hinderin with SMC3. A) The five-domain structure of Hinderin is compared to that of SMC3. The different structural domains are drawn in scale to allow a direct comparison of the size of the terminal globular regions, the two coiled-coil domains and the central globular domain in the two proteins. B) Mode of interaction of the SMC1-SMC3 dimer. The juxtaposition of the cohesins hinge domains interacting through sites located at the globular-coiled coil domain boundaries (ref. 6) is illustrated. C) Postulated mechanism for the competitive binding of Hinderin to the hinge domain of SMC3. The N- and C-terminal globular domains of Hinderin are shown to interact with binding sites located on the SMC3 hinge. The Hinderin central globular domain is not involved in the binding to SMC3 but may play a role by orienting the N- and C-terminal globular domains toward their targets.
Patel and Ghiselli BMC Cell Biology 2005 6:3 doi:10.1186/1471-2121-6-3