InterPro domain: IPR007052

The bipartite CS domain, which was named after CHORD-containing proteins and SGT1 [ 1 ], is a ~100-residue protein-protein interaction module. The CS domain can be found in stand-alone form, as well as fused with other domains, such as CHORD ( IPR007051 ), SGS ( IPR007699 ), TPR ( IPR019734 ), cytochrome b5 ( IPR001199 ) or b5 reductase, in multidomain proteins [ 2 ].

The CS domain has a compact antiparallel beta-sandwich fold consisting of seven beta-strands [ 3 , 3 ].

Some proteins known to contain a CS domain are listed below [ 4 ]:

• Eukaryotic proteins of the SGT1 family.
• Eukaryotic Rar1, related to pathogenic resistance in plants, and to development in animals.
• Eukaryotic nuclear movement protein nudC.
• Eukaryotic proteins of the p23/wos2 family, which act as co-chaperone.
• Animal b5+b5R flavo-hemo cytochrome NAD(P)H oxydoreductase type B.
• Mammalian integrin beta-1-binding protein 2 (melusin).

1. A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans. Cell 99, 355-66
2. p23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families. FEBS Lett. 529, 162-7
3. Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. J. Biol. Chem. 279, 16511-7