Fibrillin: From domain structure to supramolecular assembly

Matrix Biology

Volumn 19, Issue 6, 2000, Pages 457-470

  Handford, P A ^a   Downing, A K ^a   Reinhardt, D P ^b   Sakai, L Y ^c  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF LÜBECK   (Germany)

^c OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

Fibrillin; Function; Structure

Indexed keywords

FIBRILLIN;

CHEMICAL STRUCTURE; HUMAN; MISSENSE MUTATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; PROTEIN STRUCTURE, FUNCTION AND VARIABILITY; REVIEW;

EID: 0033783214     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(00)00100-1     Document Type: Short Survey

References (51)

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4. Revised genomic organization of FBN1 and significance for regulated gene expression
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12. Atomic force microscopy and modeling of natural elastic fibrillin polymers
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14. Fibrillin-1 in human cartilage: developmental expression and formation of special banded fibers
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20. MOISCRIPT: a program to produce both detailed and schematic plots of protein structures
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34. Calcium stabilizes fibrillin-1 against proteolytic degradation
35. Calcium determines the shape of fibrillin
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38. Association of the small latent transforming growth factor-β with an eight cysteine repeat of its binding protein (LTBP-1)
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40. EGF-like domain calcium affinity modulated by N-terminal domain linkage in human fibrillin-1
41. The high affinity calcium-binding sites in the epidermal growth factor module region of vitamin K-dependent protein S
42. EGF-like module pair 3-4 in vitamin K-dependent protein S: modulation of calcium affinity of module 4 by module 3, and interaction with factor X
43. N-terminal domains of fibrillin 1 and fibrillin 2 direct the formation of homodimers: a possible first step in microfibril assembly
44. Calcium determines the supramolecular organization of fibrillin-rich microfibrils
45. NMR analysis of cbEGF domains gives new insights into the structural consequences of a P1148A substitution in fibrillin-1
46. A Gly→Ser change causes defective folding in vitro of calcium-binding epidermal growth factor-like domains from factor IX and fibrillin-1
47. Fibrillin domain folding and calcium binding: significance to Marfan syndrome
48. Solution structure of the transforming growth factor β-binding protein-like module, a domain associated with matrix fibrils