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Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation.

ABSTRACT: 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 ??-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.

SUBMITTER: Taler-Vercic A

PROVIDER: S-EPMC5372565 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation.

Taler-Verčič Ajda A Hasanbašić Samra S Berbić Selma S Stoka Veronika V Turk Dušan D Žerovnik Eva E

International journal of molecular sciences 20170307 3

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 amy ...[more]

PMID: 28272335

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