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Evolution of fold switching in a metamorphic protein.
Dishman, Acacia F; Tyler, Robert C; Fox, Jamie C; Kleist, Andrew B; Prehoda, Kenneth E; Babu, M Madan; Peterson, Francis C; Volkman, Brian F.
Afiliación
  • Dishman AF; Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, USA.
  • Tyler RC; Medical Scientist Training Program, Medical College of Wisconsin, Milwaukee, WI, USA.
  • Fox JC; Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, USA.
  • Kleist AB; Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, USA.
  • Prehoda KE; Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, USA.
  • Babu MM; Medical Scientist Training Program, Medical College of Wisconsin, Milwaukee, WI, USA.
  • Peterson FC; Institute of Molecular Biology, Department of Chemistry and Biochemistry, University of Oregon, Eugene, OR, USA.
  • Volkman BF; MRC Laboratory of Molecular Biology, Cambridge, UK.
Science ; 371(6524): 86-90, 2021 01 01.
Article en En | MEDLINE | ID: mdl-33384377
Metamorphic proteins switch between different folds, defying the protein folding paradigm. It is unclear how fold switching arises during evolution. With ancestral reconstruction and nuclear magnetic resonance, we studied the evolution of the metamorphic human protein XCL1, which has two distinct folds with different functions, making it an unusual member of the chemokine family, whose members generally adopt one conserved fold. XCL1 evolved from an ancestor with the chemokine fold. Evolution of a dimer interface, changes in structural constraints and molecular strain, and alteration of intramolecular protein contacts drove the evolution of metamorphosis. Then, XCL1 likely evolved to preferentially populate the noncanonical fold before reaching its modern-day near-equal population of folds. These discoveries illuminate how one sequence has evolved to encode multiple structures, revealing principles for protein design and engineering.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ingeniería de Proteínas / Pliegue de Proteína / Evolución Molecular / Quimiocinas C Límite: Humans Idioma: En Revista: Science Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Imprimir
XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ingeniería de Proteínas / Pliegue de Proteína / Evolución Molecular / Quimiocinas C Límite: Humans Idioma: En Revista: Science Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos