1b0w: Difference between revisions
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[[Image:1b0w.gif|left|200px]] | [[Image:1b0w.gif|left|200px]] | ||
'''Structural comparison of amyloidogenic light chain dimer in two crystal forms with nonamyloidogenic counterparts''' | {{Structure | ||
|PDB= 1b0w |SIZE=350|CAPTION= <scene name='initialview01'>1b0w</scene>, resolution 1.80Å | |||
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'''Structural comparison of amyloidogenic light chain dimer in two crystal forms with nonamyloidogenic counterparts''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1B0W is a [ | 1B0W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B0W OCA]. | ||
==Reference== | ==Reference== | ||
Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation., Schormann N, Murrell JR, Benson MD, Amyloid. 1998 Sep;5(3):175-87. PMID:[http:// | Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation., Schormann N, Murrell JR, Benson MD, Amyloid. 1998 Sep;5(3):175-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9818054 9818054] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:04:50 2008'' | ||
Revision as of 08:04, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Structural comparison of amyloidogenic light chain dimer in two crystal forms with nonamyloidogenic counterparts
Overview
The most common form of hereditary systemic amyloidosis is familial amyloidotic polyneuropathy associated with single amino acid changes in the plasma protein transthyretin. So far, high resolution structures of only three amyloidogenic variants (Met30, Ser84, Ile122) and one non-amyloidogenic variant (Thr109) have been reported complemented by X-ray fiber diffraction studies and image reconstruction from electron micrographs of amyloid fibrils. To investigate the role of structural factors in this disease, we extended our studies to other transthyretin variants. We report crystallization and structural investigations of three amyloidogenic (Arg10, Ala60, Tyr77) and two non-amyloidogenic variants (Ser6, Met119). The similarity of these structures to normal transthyretin does not give direct clues to the fibril forming process. Since transthyretin amyloid fibrils contain a major fragment starting at position 49, besides the intact molecule, we calculated the solvent accessibility of residue 48. Indeed, all amyloidogenic variants show an increased main chain solvent exposure when compared to normal transthyretin and non-amyloidogenic variants, which can be postulated to result in increased susceptibility to proteolysis. After limited proteolysis, dimers are incapable of reassociation to native tetramers. We present a model for amyloid fibril formation based on formation of fibrils from N-terminal truncated dimers as building blocks.
About this Structure
1B0W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation., Schormann N, Murrell JR, Benson MD, Amyloid. 1998 Sep;5(3):175-87. PMID:9818054
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