Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties

Bourne, P. C., Ramsland, P. A., Shan, L., Fan, Z. C., DeWitt, C. R., Shultz, B. B., Terzyan, S. S., Moomaw, C. R., Slaughter, C. A., Guddat, L. W. and Edmundson, A. B. (2002) Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties. Acta Crystallographica Section D: Biological Crystallography, 58 5: 815-823. doi:10.1107/S0907444902004183

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Author Bourne, P. C.
Ramsland, P. A.
Shan, L.
Fan, Z. C.
DeWitt, C. R.
Shultz, B. B.
Terzyan, S. S.
Moomaw, C. R.
Slaughter, C. A.
Guddat, L. W.
Edmundson, A. B.
Title Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties
Journal name Acta Crystallographica Section D: Biological Crystallography   Check publisher's open access policy
ISSN 0907-4449
Publication date 2002
Sub-type Article (original research)
DOI 10.1107/S0907444902004183
Open Access Status File (Publisher version)
Volume 58
Issue 5
Start page 815
End page 823
Total pages 9
Place of publication Copenhagen
Publisher Blackwell Munksgaard
Language eng
Abstract The X-ray structure of an immunoglobulin light-chain dimer isolated from the urine as a 'Bence-Jones protein' from a patient with multiple myeloma and amyloidosis (Sea) was determined at 1.94 Angstrom resolution and refined to R and R-free factors of 0.22 and 0.25, respectively. This 'amyloidogenic' protein crystallized in the orthorhombic P2(1)2(1)2(1) space group with unit-cell parameters a=48.28, b=83.32, c=112.59 Angstrom as determined at 100 K. In the vital organs (heart and kidneys), the equivalent of the urinary protein produced fibrillar amyloid deposits which were fatal to the patient. Compared with the amyloidogenic Mcg light-chain dimer, the Sea protein was highly soluble in aqueous solutions and only crystallized at concentrations approaching 100 mg ml(-1). Both the Sea and Mcg proteins packed into crystals in highly ordered arrangements typical of strongly diffracting crystals of immunoglobulin fragments. Overall similarities and significant differences in the three-dimensional structures and crystalline properties are discussed for the Sea and Mcg Bence-Jones proteins, which together provide a generalized model of abnormalities present in lambda chains, facilitating a better understanding of amyloidosis of light-chain origin (AL).
Keyword Biochemical Research Methods
Biochemistry & Molecular Biology
Biophysics
Crystallography
Bence-jones Proteins
X-ray-diffraction
Al Amyloidosis
In-vitro
Binding
Mcg
Fibrils
Fibrillogenesis
Crystallize
Deposition
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
 
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Created: Wed, 19 Sep 2007, 16:47:03 EST