Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily

EMBO Journal

Volumn 20, Issue 17, 2001, Pages 4774-4781

  Staniforth, Rosemary A ^a   Giannini, Silva ^a   Higgins, Lee D ^a   Conroy, Matthew J ^a   Hounslow, Andrea M ^a   Jerala, Roman ^b   Craven, C Jeremy ^a   Waltho, Jonathan P ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

^b NATIONAL INSTITUTE OF CHEMISTRY   (Slovenia)

Author keywords

Amyloid; Cystatin; Domain swapping; Molten globule

Indexed keywords

AMYLOID; CYSTATIN;

ARTICLE; CONFORMATIONAL TRANSITION; DIMERIZATION; GENE MUTATION; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; CHICKENS; CYSTATINS; DIMERIZATION; GUANIDINE; HUMANS; HYDROGEN BONDING; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; THERMODYNAMICS;

GALLUS GALLUS;

EID: 0035801540     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.17.4774     Document Type: Article

References (47)

1. Molecular basis for amyloidosis related to hereditary brain hemorrhage
2. Increased body temperature accelerates aggregation of the Leu-68→G1n mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy
3. Cystatin, a protein inhibitor of cyteine proteinases-improved purification from egg-white
4. The cystatins-a new class of peptidase inhibitors
5. Biphasic transition curve on denaturation of chicken cystatin by guanidinium chloride-evidence for an independently unfolding structural region
6. Different roles of the 2 disulfide bonds of the cysteine proteinase inhibitor, chicken cystatin, for the conformation of the active protein
7. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
8. Conformational changes and disease-serpins, prions and Alzheimer's
9. Pathologic conformations of the prion proteins
10. Protein backbone angle restraints from searching a database for chemical shift and sequence homology
11. Identification of amino acid residues critical for aggregation of human CC chemokines macrophage inflammatory protein (MIP)-1 α, MIP-1 β and RANTES - Characterization of active disaggregated chemokine variants
12. Folding-related dimerization of human cystatin C
13. NMR structural studies of human cystatin C dimers and monomers
14. Conformational variability of chicken cystatin-comparison of structures determined by X-ray diffraction and NMR spectroscopy
15. Assembly of Ap amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease
16. Engineered assembly of intertwined oligomers of an immuno-globulin chain
17. Multiple folding pathways for heterologously expressed human prion protein
18. Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain-swapping
19. Hereditary cystatin C (γ-trace) amyloid angiopathy of the CNS causing cerebral hemorrhage
20. Accessing the global minimum conformation of stefin A dimer by annealing under partially denaturing conditions
21. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
22. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
23. Amyloid-like aggregates of a plant protein: A case of a sweet-tasting protein, monellin
24. MOLSCRIPT-a program to produce both detailed and schematic plots of protein structures
25. The crystal structure of a 3D domain-swapped dimer of Rnase A at a 2.1 Å resolution
26. The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions
27. The 3-dimensional solution structure of human stefin A
28. RASTER3D version 2.0 - A program for photorealistic molecular graphics
29. Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors
30. Ambiguous distance data in the calculation of NMR structures
31. 15N labeling of proteins
32. An integrated kinetic-analysis of intermediates and transition states in protein folding reactions
33. Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues
34. Cryo electron microscopy of amyloid fibrils
35. TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins
36. Conformational changes and disease-serpins, prions and Alzheimer's
37. Nucleated conformational conversion and the replication of conformational information by a prion determinant
38. The major transition state in folding need not involve the immobilization of side chains
39. The refined 2.4 Å X-ray crystal structure of recombinant human stefin B in complex with the cyteine proteinase papain - A novel type of proteinase-inhibitor interaction
40. The structure of amyloid fibrils by electron microscopy and X-ray diffraction
41. Common core structure of amyloid fibrils by synchrotron X-ray diffraction
42. 15N labeling of proteins for NMR studies
43. Amyloid O-protein fibrillogenesis-detection of a protofibrillar intermediate
44. Trimeric domain-swapped barnase
45. Characterization of the equilibrium intermediates in acid denaturation of human stefin B