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. Author manuscript; available in PMC: 2016 May 14.
Published in final edited form as: Curr Biol. 2009 Dec 29;19(24):R1126–R1132. doi: 10.1016/j.cub.2009.10.067

Figure 1. Cohesin complex assembly and structure.

Figure 1

SMCs contain long helical domains interrupted by a centrally positioned hinge. Hinge folding enables the helical domains to intertwine in an anti-parallel fashion and form a stable coiled-coil rod-like structure. Folding over also brings amino- and carboxy-terminal globular ATPase domains for each SMC into registration. Smc1/3 bind together by dimerization of hinge domains and by association of globular head domains. The Smc1/3 ATPase domains are capped by Mcd1/Scc1. Mcd1/Scc1 recruits Scc3/Irr1.