Metamorphic Proteins

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Conformations of Lymphotactin in Equilibrium

Metamorphic proteins ( English : metamorphic proteins ) are proteins , in addition to intrinsically unstructured proteins unstructured in themselves and in multiple conformations may be present. All possible conformations of the protein have approximately the same Gibbs energy and are in equilibrium. They are able to adopt different protein folds for the same amino acid sequence under native conditions . Metamorphic proteins can only develop their function when they bind to small molecules or other proteins.

The best-known metamorphic protein is lymphotactin , a cytokine . The chemokine structure of lymphotactin is characteristic of chemokines due to the three - stranded β-sheet and the C -terminal helix . This structure is used to bind and activate your receptor. The identical dimer is the glycosaminoglycan-binding structure that can bind to glycosaminoglycans , more precisely to heparins , and consists only of β-sheets. The mutual activity of the conformations is important for the complete function of metamorphic proteins in vivo .

Individual evidence

  1. Jeremy M. Berg, Lubert Stryer , John L. Tymoczko: Stryer Biochemistry . 7th edition. Springer-Verlag, Berlin / Heidelberg 2013, ISBN 978-3-8274-2988-9 , pp. 56 .
  2. Alexey G. Murzin: Metamorphic Proteins . In: Science . tape 320 , no. 5884 , June 27, 2008, ISSN  0036-8075 , p. 1725–1726 , doi : 10.1126 / science.1158868 , PMID 18583598 ( sciencemag.org [accessed July 6, 2017]).