AI Article Synopsis
- The structure of stefin B is identified as a tetramer formed by the interaction of two domain-swapped dimers.
- The transformation includes a novel process called "hand shaking," occurring alongside the isomerization of proline 74 from trans to cis.
- This proline is highly conserved in the cystatin family and may be crucial in the development of conditions like cerebral amyloid angiopathy, suggesting the broader importance of proline isomerization in amyloid formation.
Article 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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| http://dx.doi.org/10.1016/j.jmb.2006.12.025 | DOI Listing |
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