摘要: An atomic model for the rigor complex of F-actin and myosin head has been obtained by combining molecular structures individual proteins (Rayment et al. 1993a) (Holmes 1990) (Lorenz 1993) with low resolution electron density maps actomyosin derived cryoelectron microscopy 1993b) (Schroder 1993). A interaction proposed in which actin binding sites nucleotide SI are functionally linked a cleft 50K domain is thought to close on 1993b). The closing likely be an essential part weak/strong sequence interaction. initial probably involves only surface, full develops closure cleft. obligatory sequencestereo specific-weak/strong prevents cross-bridge from unstrained strong state. Tropomyosin “off” state appears inhibit
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