1ihm
From Proteopedia
(New page: 200px<br /><applet load="1ihm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ihm, resolution 3.4Å" /> '''CRYSTAL STRUCTURE ANA...) |
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| - | [[Image:1ihm.gif|left|200px]]<br /><applet load="1ihm" size=" | + | [[Image:1ihm.gif|left|200px]]<br /><applet load="1ihm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ihm, resolution 3.4Å" /> | caption="1ihm, resolution 3.4Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSID'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSID'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Norwalk virus, a noncultivatable human calicivirus, is the major cause of | + | Norwalk virus, a noncultivatable human calicivirus, is the major cause of epidemic gastroenteritis in humans. The first x-ray structure of a calicivirus capsid, which consists of 180 copies of a single protein, has been determined by phase extension from a low-resolution electron microscopy structure. The capsid protein has a protruding (P) domain connected by a flexible hinge to a shell (S) domain that has a classical eight-stranded beta-sandwich motif. The structure of the P domain is unlike that of any other viral protein with a subdomain exhibiting a fold similar to that of the second domain in the eukaryotic translation elongation factor-Tu. This subdomain, located at the exterior of the capsid, has the largest sequence variation among Norwalk-like human caliciviruses and is likely to contain the determinants of strain specificity and cell binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1IHM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Norwalk_virus Norwalk virus]. Full crystallographic information is available from [http:// | + | 1IHM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Norwalk_virus Norwalk virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IHM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bella, J.]] | [[Category: Bella, J.]] | ||
[[Category: Dokland, T.]] | [[Category: Dokland, T.]] | ||
| - | [[Category: Estes, M | + | [[Category: Estes, M K.]] |
| - | [[Category: Hardy, M | + | [[Category: Hardy, M E.]] |
| - | [[Category: Prasad, B | + | [[Category: Prasad, B V.]] |
| - | [[Category: Rossmann, M | + | [[Category: Rossmann, M G.]] |
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
[[Category: ef-tu-like domain caliciviridae]] | [[Category: ef-tu-like domain caliciviridae]] | ||
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[[Category: t=3 icosahedral capsid]] | [[Category: t=3 icosahedral capsid]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:58 2008'' |
Revision as of 11:11, 21 February 2008
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CRYSTAL STRUCTURE ANALYSIS OF NORWALK VIRUS CAPSID
Overview
Norwalk virus, a noncultivatable human calicivirus, is the major cause of epidemic gastroenteritis in humans. The first x-ray structure of a calicivirus capsid, which consists of 180 copies of a single protein, has been determined by phase extension from a low-resolution electron microscopy structure. The capsid protein has a protruding (P) domain connected by a flexible hinge to a shell (S) domain that has a classical eight-stranded beta-sandwich motif. The structure of the P domain is unlike that of any other viral protein with a subdomain exhibiting a fold similar to that of the second domain in the eukaryotic translation elongation factor-Tu. This subdomain, located at the exterior of the capsid, has the largest sequence variation among Norwalk-like human caliciviruses and is likely to contain the determinants of strain specificity and cell binding.
About this Structure
1IHM is a Single protein structure of sequence from Norwalk virus. Full crystallographic information is available from OCA.
Reference
X-ray crystallographic structure of the Norwalk virus capsid., Prasad BV, Hardy ME, Dokland T, Bella J, Rossmann MG, Estes MK, Science. 1999 Oct 8;286(5438):287-90. PMID:10514371
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