HADDOCK-derived structure of the CH-domain of the smoothelin-like 1 complexed with the C-domain of apocalmodulin
Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: a unique apocalmodulin-binding mode and the possible role of the C-terminal type-2 CH-domain in smooth muscle relaxation.
GPLGSKNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQL LEVDDMVRLAVPDSKCVYTYIQELYRSLVQKGLVKTKKK
0.5 mM [U-100% 15N] entity_1, 0.6 mM calmodulin (full length), 20 mM Bis-Tris, 0.5 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 1 mM EDTA, 90% H2O/10% D2O
0.6 mM entity_1, 0.5 mM [U-100% 15N] calmodulin (full length), 20 mM Bis-Tris, 0.5 mM DSS, 10 mM [U-2H] DTT, 0.03 % sodium azide, 1 mM EDTA, 90% H2O/10% D2O
apocalmodulin complex, calponin homology domain, smoothelin-like 1, HADDOCK model, CH-domain, Coiled coil, Acetylation, Calcium, Methylation, PROTEIN BINDING
KNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDD MVRLAVPDSKCVYTYIQELYRSLVQKGLVKTKKK