Essential Role of Proline Isomerization in Stefin B Tetramer Formation

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...

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Bibliographic Details
Published inJournal of molecular biology Vol. 366; no. 5; pp. 1569 - 1579
Main Authors Jenko Kokalj, Saša, Gunčar, Gregor, Štern, Igor, Morgan, Gareth, Rabzelj, Sabina, Kenig, Manca, Staniforth, Rosemary A., Waltho, Jonathan P., Žerovnik, Eva, Turk, Dušan
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 09.03.2007
Subjects
Amino Acid Sequence
Amino Acid Substitution
amyloid
Amyloid - chemistry
Amyloid - metabolism
Amyloid - ultrastructure
Circular Dichroism
Cross-Linking Reagents
crystal structure
Crystallography, X-Ray
cystatin
Cystatin B
Cystatins - chemistry
Cystatins - genetics
Cystatins - metabolism
Dimerization
domain-swapping
Genetic Variation
Glutaral - chemistry
Humans
Hydrogen-Ion Concentration
Isomerism
Light
Models, Chemical
Models, Molecular
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Proline - chemistry
Proline - metabolism
Protein Conformation
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Scattering, Radiation
Sequence Homology, Amino Acid
Serine - metabolism
Solutions - chemistry
stefin
Trifluoroethanol - pharmacology
SEC
domain-swapping
ThT
amyloid
AFM
stefin
crystal structure
cystatin
TEM
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2006.12.025