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10.1073/pnas.2115001118

http://scihub22266oqcxt.onion/10.1073/pnas.2115001118
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34620716!8521671!34620716
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suck abstract from ncbi


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pmid34620716      Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (41): ä
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  • Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (Legobodies) #MMPMID34620716
  • Wu X; Rapoport TA
  • Proc Natl Acad Sci U S A 2021[Oct]; 118 (41): ä PMID34620716show ga
  • We describe a general method that allows structure determination of small proteins by single-particle cryo-electron microscopy (cryo-EM). The method is based on the availability of a target-binding nanobody, which is then rigidly attached to two scaffolds: 1) a Fab fragment of an antibody directed against the nanobody and 2) a nanobody-binding protein A fragment fused to maltose binding protein and Fab-binding domains. The overall ensemble of approximately 120 kDa, called Legobody, does not perturb the nanobody-target interaction, is easily recognizable in EM images due to its unique shape, and facilitates particle alignment in cryo-EM image processing. The utility of the method is demonstrated for the KDEL receptor, a 23-kDa membrane protein, resulting in a map at 3.2-A overall resolution with density sufficient for de novo model building, and for the 22-kDa receptor-binding domain (RBD) of SARS-CoV-2 spike protein, resulting in a map at 3.6-A resolution that allows analysis of the binding interface to the nanobody. The Legobody approach thus overcomes the current size limitations of cryo-EM analysis.
  • |Binding Sites/immunology[MESH]
  • |COVID-19/virology[MESH]
  • |Cryoelectron Microscopy/*methods[MESH]
  • |HEK293 Cells[MESH]
  • |Humans[MESH]
  • |Models, Molecular[MESH]
  • |Protein Binding[MESH]
  • |Protein Domains[MESH]
  • |SARS-CoV-2/immunology/*metabolism/physiology[MESH]
  • |Single-Domain Antibodies/immunology/*metabolism[MESH]


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