1g96
From Proteopedia
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'''HUMAN CYSTATIN C; DIMERIC FORM WITH 3D DOMAIN SWAPPING''' | '''HUMAN CYSTATIN C; DIMERIC FORM WITH 3D DOMAIN SWAPPING''' | ||
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[[Category: Kozak, M.]] | [[Category: Kozak, M.]] | ||
[[Category: 3d domain swapping]] | [[Category: 3d domain swapping]] | ||
| - | [[Category: | + | [[Category: Amyloid angiopathy and cerebral hemorrhage]] |
| - | [[Category: | + | [[Category: Amyloid formation]] |
| - | [[Category: | + | [[Category: Human cystatin c dimer]] |
| - | [[Category: | + | [[Category: Inhibitor of c1 and c13 cysteine protease]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:18:07 2008'' | |
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Revision as of 14:18, 2 May 2008
HUMAN CYSTATIN C; DIMERIC FORM WITH 3D DOMAIN SWAPPING
Overview
The crystal structure of human cystatin C, a protein with amyloidogenic properties and a potent inhibitor of cysteine proteases, reveals how the protein refolds to produce very tight two-fold symmetric dimers while retaining the secondary structure of the monomeric form. The dimerization occurs through three-dimensional domain swapping, a mechanism for forming oligomeric proteins. The reconstituted monomer-like domains are similar to chicken cystatin except for one inhibitory loop that unfolds to form the 'open interface' of the dimer. The structure explains the tendency of human cystatin C to dimerize and suggests a mechanism for its aggregation in the brain arteries of elderly people with amyloid angiopathy. A more severe 'conformational disease' is associated with the L68Q mutant of human cystatin C, which causes massive amyloidosis, cerebral hemorrhage and death in young adults. The structure of the three-dimensional domain-swapped dimers shows how the L68Q mutation destabilizes the monomers and makes the partially unfolded intermediate less unstable. Higher aggregates may arise through the three-dimensional domain-swapping mechanism occurring in an open-ended fashion in which partially unfolded molecules are linked into infinite chains.
About this Structure
1G96 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping., Janowski R, Kozak M, Jankowska E, Grzonka Z, Grubb A, Abrahamson M, Jaskolski M, Nat Struct Biol. 2001 Apr;8(4):316-20. PMID:11276250 Page seeded by OCA on Fri May 2 17:18:07 2008
