1g96

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{{STRUCTURE_1g96| PDB=1g96 | SCENE= }}
{{STRUCTURE_1g96| PDB=1g96 | SCENE= }}
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'''HUMAN CYSTATIN C; DIMERIC FORM WITH 3D DOMAIN SWAPPING'''
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===HUMAN CYSTATIN C; DIMERIC FORM WITH 3D DOMAIN SWAPPING===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11276250 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11276250}}
==About this Structure==
==About this Structure==
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[[Category: Human cystatin c dimer]]
[[Category: Human cystatin c dimer]]
[[Category: Inhibitor of c1 and c13 cysteine protease]]
[[Category: Inhibitor of c1 and c13 cysteine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:18:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:56:36 2008''

Revision as of 01:56, 1 July 2008

Image:1g96.png

Template:STRUCTURE 1g96

HUMAN CYSTATIN C; DIMERIC FORM WITH 3D DOMAIN SWAPPING

Template:ABSTRACT PUBMED 11276250

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

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