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1g96
From Proteopedia
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|PDB= 1g96 |SIZE=350|CAPTION= <scene name='initialview01'>1g96</scene>, resolution 2.5Å | |PDB= 1g96 |SIZE=350|CAPTION= <scene name='initialview01'>1g96</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1cew|1cew]], [[1stf|1stf]], [[1a67|1a67]], [[1dvc|1dvc]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g96 OCA], [http://www.ebi.ac.uk/pdbsum/1g96 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g96 RCSB]</span> | ||
}} | }} | ||
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[[Category: Jaskolski, M.]] | [[Category: Jaskolski, M.]] | ||
[[Category: Kozak, M.]] | [[Category: Kozak, M.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: GOL]] | ||
[[Category: 3d domain swapping]] | [[Category: 3d domain swapping]] | ||
[[Category: amyloid angiopathy and cerebral hemorrhage]] | [[Category: amyloid angiopathy and cerebral hemorrhage]] | ||
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[[Category: inhibitor of c1 and c13 cysteine protease]] | [[Category: inhibitor of c1 and c13 cysteine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:39:15 2008'' |
Revision as of 17:39, 30 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1cew, 1stf, 1a67, 1dvc
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 20:39:15 2008
