| Autor: |
Ajda Taler-Verčič, Samra Hasanbašić, Selma Berbić, Veronika Stoka, Dušan Turk, Eva Žerovnik |
| Jazyk: |
angličtina |
| Rok vydání: |
2017 |
| Předmět: |
|
| Zdroj: |
International Journal of Molecular Sciences, Vol 18, Iss 3, p 549 (2017) |
| Druh dokumentu: |
article |
| ISSN: |
1422-0067 |
| DOI: |
10.3390/ijms18030549 |
| Popis: |
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 β2-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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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