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.


1g5g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1g5g.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1g5g.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1g5g| PDB=1g5g | SCENE= }}
{{STRUCTURE_1g5g| PDB=1g5g | SCENE= }}
-
'''FRAGMENT OF FUSION PROTEIN FROM NEWCASTLE DISEASE VIRUS'''
+
===FRAGMENT OF FUSION PROTEIN FROM NEWCASTLE DISEASE VIRUS===
-
==Overview==
+
<!--
-
BACKGROUND: Membrane fusion within the Paramyxoviridae family of viruses is mediated by a surface glycoprotein termed the "F", or fusion, protein. Membrane fusion is assumed to involve a series of structural transitions of F from a metastable (prefusion) state to a highly stable (postfusion) state. No detail is available at the atomic level regarding the metastable form of these proteins or regarding the transitions accompanying fusion. RESULTS: The three-dimensional structure of the fusion protein of Newcastle disease virus (NDV-F) has been determined. The trimeric NDV-F molecule is organized into head, neck, and stalk regions. The head is comprised of a highly twisted beta domain and an additional immunoglobulin-like beta domain. The neck is formed by the C-terminal extension of the heptad repeat region HR-A, capped by a four-helical bundle. The C terminus of HR-A is encased by a further helix HR-C and a 4-stranded beta sheet. The stalk is formed by the remaining visible portion of HR-A and by polypeptide immediately N-terminal to the C-terminal heptad repeat region HR-B. An axial channel extends through the head and neck and is fenestrated by three large radial channels located approximately at the head-neck interface. CONCLUSION: We propose that prior to fusion activation, the hydrophobic fusion peptides in NDV-F are sequestered within the radial channels within the head, with the central HR-A coiled coil being only partly formed. Fusion activation then involves, inter alia, the assembly of a complete HR-A coiled coil, with the fusion peptides and transmembrane anchors being brought into close proximity. The structure of NDV-F is fundamentally different than that of influenza virus hemagglutinin, in that the central coiled coil is in the opposite orientation with respect to the viral membrane.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11286892}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11286892 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11286892}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Newcastle disease virus]]
[[Category: Newcastle disease virus]]
[[Category: Paramyxovirus]]
[[Category: Paramyxovirus]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:09:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:27:58 2008''

Revision as of 01:28, 1 July 2008

Image:1g5g.png

Template:STRUCTURE 1g5g

FRAGMENT OF FUSION PROTEIN FROM NEWCASTLE DISEASE VIRUS

Template:ABSTRACT PUBMED 11286892

About this Structure

1G5G is a Single protein structure of sequence from Newcastle disease virus. Full crystallographic information is available from OCA.

Reference

The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion., Chen L, Gorman JJ, McKimm-Breschkin J, Lawrence LJ, Tulloch PA, Smith BJ, Colman PM, Lawrence MC, Structure. 2001 Mar 7;9(3):255-66. PMID:11286892

Page seeded by OCA on Tue Jul 1 04:27:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g5g"
Personal tools