2oct: Difference between revisions

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[[Image:2oct.gif|left|200px]]
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[[Image:2oct.png|left|200px]]


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{{STRUCTURE_2oct|  PDB=2oct  |  SCENE=  }}  
{{STRUCTURE_2oct|  PDB=2oct  |  SCENE=  }}  


'''Stefin B (Cystatin B) tetramer'''
===Stefin B (Cystatin B) tetramer===




==Overview==
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Here we present the tetrameric structure of stefin B, which is the result of a process by which two domain-swapped dimers of stefin B are transformed into tetramers. The transformation involves a previously unidentified process of extensive intermolecular contacts, termed hand shaking, which occurs concurrently with trans to cis isomerization of proline 74. This proline residue is widely conserved throughout the cystatin superfamily, a member of which, human cystatin C, is the key protein in cerebral amyloid angiopathy. These results are consistent with the hypothesis that isomerization of proline residues can play a decisive role in amyloidogenesis.
The line below this paragraph, {{ABSTRACT_PUBMED_17217964}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_17217964}}


==Disease==
==Disease==
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[[Category: Proline isomerization]]
[[Category: Proline isomerization]]
[[Category: Stefin]]
[[Category: Stefin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:20:52 2008''

Revision as of 05:20, 29 July 2008

File:2oct.png

Template:STRUCTURE 2oct

Stefin B (Cystatin B) tetramer

Template:ABSTRACT PUBMED 17217964

Disease

Known disease associated with this structure: Epilepsy, progressive myoclonic 1 OMIM:[601145]

About this Structure

2OCT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Essential role of proline isomerization in stefin B tetramer formation., Jenko Kokalj S, Guncar G, Stern I, Morgan G, Rabzelj S, Kenig M, Staniforth RA, Waltho JP, Zerovnik E, Turk D, J Mol Biol. 2007 Mar 9;366(5):1569-79. Epub 2006 Dec 16. PMID:17217964

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