Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 18, Issue 3, Pages -Publisher
MDPI AG
DOI: 10.3390/ijms18030549
Keywords
cis proline; conformational switch; folding intermediate; domain swapping; amyloid fibrils; protein aggregation; stefin B; beta(2)-microglobulin
Funding
- Slovenian Research Agency [P1-0048, P1-0140]
- CMEPIUS
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Here we discuss studies of the structure, folding, oligomerization and amyloid fibril formation of several proline mutants of human stefin B, which is a protein inhibitor of lysosomal cysteine cathepsins and a member of the cystatin family. The structurally important prolines in stefin B are responsible for the slow folding phases and facilitate domain swapping (Pro 74) and loop swapping (Pro 79). Moreover, our findings are compared to beta(2)-microglobulin, a protein involved in dialysis-related amyloidosis. The assessment of the contribution of proline residues to the process of amyloid fibril formation may shed new light on the critical molecular events involved in conformational disorders.
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