Essential role of proline isomerization in stefin B tetramer formation |
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Authors: | Jenko Kokalj Sasa Guncar Gregor Stern Igor Morgan Gareth Rabzelj Sabina Kenig Manca Staniforth Rosemary A Waltho Jonathan P Zerovnik Eva Turk Dusan |
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Institution: | Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia. |
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Abstract: | Here we present the tetrameric structure of stefin B, which is the result of a process by which two domain-swapped dimers of stefin B are transformed into tetramers. The transformation involves a previously unidentified process of extensive intermolecular contacts, termed hand shaking, which occurs concurrently with trans to cis isomerization of proline 74. This proline residue is widely conserved throughout the cystatin superfamily, a member of which, human cystatin C, is the key protein in cerebral amyloid angiopathy. These results are consistent with the hypothesis that isomerization of proline residues can play a decisive role in amyloidogenesis. |
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Keywords: | TEM transmission electron microscopy AFM atomic force microscopy SEC size-exclusion chromatography ThT thioflavine T |
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