This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ihm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1ihm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ihm, resolution 3.4&Aring;" /> '''CRYSTAL STRUCTURE ANA...)
Line 1: Line 1:
-
[[Image:1ihm.gif|left|200px]]<br /><applet load="1ihm" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ihm.gif|left|200px]]<br /><applet load="1ihm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ihm, resolution 3.4&Aring;" />
caption="1ihm, resolution 3.4&Aring;" />
'''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, 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.
+
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IHM OCA].
+
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==
Line 15: Line 15:
[[Category: Bella, J.]]
[[Category: Bella, J.]]
[[Category: Dokland, T.]]
[[Category: Dokland, T.]]
-
[[Category: Estes, M.K.]]
+
[[Category: Estes, M K.]]
-
[[Category: Hardy, M.E.]]
+
[[Category: Hardy, M E.]]
-
[[Category: Prasad, B.V.]]
+
[[Category: Prasad, B V.]]
-
[[Category: Rossmann, M.G.]]
+
[[Category: Rossmann, M G.]]
[[Category: beta-barrel]]
[[Category: beta-barrel]]
[[Category: ef-tu-like domain caliciviridae]]
[[Category: ef-tu-like domain caliciviridae]]
Line 24: Line 24:
[[Category: t=3 icosahedral capsid]]
[[Category: t=3 icosahedral capsid]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:02:09 2007''
+
''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


1ihm, resolution 3.4Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 13:11:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools