2oct
From Proteopedia
(New page: 200px<br /> <applet load="2oct" size="450" color="white" frame="true" align="right" spinBox="true" caption="2oct, resolution 1.4Å" /> '''Stefin B (Cystatin B...) |
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| - | [[Image:2oct.gif|left|200px]]<br /> | + | [[Image:2oct.gif|left|200px]]<br /><applet load="2oct" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2oct" size=" | + | |
caption="2oct, resolution 1.4Å" /> | caption="2oct, resolution 1.4Å" /> | ||
'''Stefin B (Cystatin B) tetramer'''<br /> | '''Stefin B (Cystatin B) tetramer'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Here we present the tetrameric structure of stefin B, which is the result | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OCT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 2OCT is a [http://en.wikipedia.org/wiki/Single_protein 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=2OCT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Guncar, G.]] | [[Category: Guncar, G.]] | ||
| - | [[Category: Kokalj, S | + | [[Category: Kokalj, S Jenko.]] |
[[Category: Turk, D.]] | [[Category: Turk, D.]] | ||
[[Category: amyloid]] | [[Category: amyloid]] | ||
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[[Category: stefin]] | [[Category: stefin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:16:58 2008'' |
Revision as of 16:16, 21 February 2008
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Stefin B (Cystatin B) tetramer
Contents |
Overview
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.
Disease
Known diseases 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
Page seeded by OCA on Thu Feb 21 18:16:58 2008
