1mec

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mec.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1mec.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mec| PDB=1mec | SCENE= }}
{{STRUCTURE_1mec| PDB=1mec | SCENE= }}
-
'''CONFORMATIONAL VARIABILITY OF A PICORNAVIRUS CAPSID: PH-DEPENDENT STRUCTURAL CHANGES OF MENGO VIRUS RELATED TO ITS HOST RECEPTOR ATTACHMENT SITE AND DISASSEMBLY'''
+
===CONFORMATIONAL VARIABILITY OF A PICORNAVIRUS CAPSID: PH-DEPENDENT STRUCTURAL CHANGES OF MENGO VIRUS RELATED TO ITS HOST RECEPTOR ATTACHMENT SITE AND DISASSEMBLY===
-
==Overview==
+
<!--
-
The structure of Mengo virus had been determined from crystals grown in the presence of 100 mM phosphate buffer at pH 7.4. It is shown that Mengo virus is poorly infectious at the phosphate concentration similar to that in which it was crystallized. Maximal infectivity is achieved at 10 mM phosphate or less in physiological saline. The phosphate effect is ameliorated when the pH is lowered to 4.6. Although it has not been possible to study the crystal structure of the virus at low phosphate concentrations, it is shown that increasing the Cl- concentration at pH 6.2 or decreasing the pH to 4.6 causes substantial conformational changes confined to the "pit," a deep surface depression. These structural changes involve a movement of the "FMDV loop" (GH loop) in VP1, an ordering of the "VP3 loop" (GH loop in VP3) between 3176 and 3182, the displacement of a bound phosphate near the "FMDV loop" (GH loop in VP1), and movement of the carboxy terminus of VP2. The changes in conformation are correlated with the dissociation of the virion into pentamers at pH 6.2 and 150 mM Cl-. The localization of the conformational changes and the correlated role of the phosphate in controlling infectivity support the hypothesis that the "pit" is the receptor attachment site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_2155508}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 2155508 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_2155508}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Cardio picornavirus coat protein]]
[[Category: Cardio picornavirus coat protein]]
[[Category: Icosahedral virus]]
[[Category: Icosahedral virus]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:56:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:47:13 2008''

Revision as of 20:47, 2 July 2008

Image:1mec.png

Template:STRUCTURE 1mec

CONFORMATIONAL VARIABILITY OF A PICORNAVIRUS CAPSID: PH-DEPENDENT STRUCTURAL CHANGES OF MENGO VIRUS RELATED TO ITS HOST RECEPTOR ATTACHMENT SITE AND DISASSEMBLY

Template:ABSTRACT PUBMED 2155508

About this Structure

1MEC is a Protein complex structure of sequences from Mengo virus. Full crystallographic information is available from OCA.

Reference

Conformational variability of a picornavirus capsid: pH-dependent structural changes of Mengo virus related to its host receptor attachment site and disassembly., Kim S, Boege U, Krishnaswamy S, Minor I, Smith TJ, Luo M, Scraba DG, Rossmann MG, Virology. 1990 Mar;175(1):176-90. PMID:2155508

Page seeded by OCA on Wed Jul 2 23:47:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mec"
Personal tools