1jvk
From Proteopedia
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[[Image:1jvk.gif|left|200px]] | [[Image:1jvk.gif|left|200px]] | ||
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'''THREE-DIMENSIONAL STRUCTURE OF AN IMMUNOGLOBULIN LIGHT CHAIN DIMER ACTING AS A LETHAL AMYLOID PRECURSOR''' | '''THREE-DIMENSIONAL STRUCTURE OF AN IMMUNOGLOBULIN LIGHT CHAIN DIMER ACTING AS A LETHAL AMYLOID PRECURSOR''' | ||
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==About this Structure== | ==About this Structure== | ||
- | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVK OCA]. | |
==Reference== | ==Reference== | ||
Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties., Bourne PC, Ramsland PA, Shan L, Fan ZC, DeWitt CR, Shultz BB, Terzyan SS, Moomaw CR, Slaughter CA, Guddat LW, Edmundson AB, Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):815-23. Epub 2002, Apr 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11976493 11976493] | Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties., Bourne PC, Ramsland PA, Shan L, Fan ZC, DeWitt CR, Shultz BB, Terzyan SS, Moomaw CR, Slaughter CA, Guddat LW, Edmundson AB, Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):815-23. Epub 2002, Apr 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11976493 11976493] | ||
- | [[Category: Homo sapiens]] | ||
- | [[Category: Protein complex]] | ||
[[Category: Bourne, P C.]] | [[Category: Bourne, P C.]] | ||
[[Category: DeWitt, C R.]] | [[Category: DeWitt, C R.]] | ||
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[[Category: Shultz, B B.]] | [[Category: Shultz, B B.]] | ||
[[Category: Terzyan, S S.]] | [[Category: Terzyan, S S.]] | ||
- | [[Category: | + | [[Category: Amyloidogenic]] |
- | [[Category: | + | [[Category: Immunoglobulin light chain dimer]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:58:43 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 18:58, 2 May 2008
THREE-DIMENSIONAL STRUCTURE OF AN IMMUNOGLOBULIN LIGHT CHAIN DIMER ACTING AS A LETHAL AMYLOID PRECURSOR
Overview
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 A 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 A 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).
About this Structure
Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties., Bourne PC, Ramsland PA, Shan L, Fan ZC, DeWitt CR, Shultz BB, Terzyan SS, Moomaw CR, Slaughter CA, Guddat LW, Edmundson AB, Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):815-23. Epub 2002, Apr 26. PMID:11976493 Page seeded by OCA on Fri May 2 21:58:43 2008