| Literature DB >> 8316857 |
I Rayment1, W R Rypniewski, K Schmidt-Bäse, R Smith, D R Tomchick, M M Benning, D A Winkelmann, G Wesenberg, H M Holden.
Abstract
Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.Entities:
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Year: 1993 PMID: 8316857 DOI: 10.1126/science.8316857
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728