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.


1onb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1onb.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1onb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1onb| PDB=1onb | SCENE= }}
{{STRUCTURE_1onb| PDB=1onb | SCENE= }}
-
'''Solution structure of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase'''
+
===Solution structure of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase===
-
==Overview==
+
<!--
-
The NS3 protein of the hepatitis C virus (HCV) is a 631 amino acid residue bifunctional enzyme with a serine protease localized to the N-terminal 181 residues and an RNA helicase located in the C-terminal 450 residues. The HCV NS3 RNA helicase consists of three well-defined subdomains which all contribute to its helicase activity. The second subdomain of the HCV helicase is flexibly linked to the remainder of the NS3 protein and could undergo rigid-body movements during the unwinding of double-stranded RNA. It also contains several motifs that are implicated in RNA binding and in coupling NTP hydrolysis to nucleic acid unwinding and translocation. As part of our efforts to use NMR techniques to assist in deciphering the enzyme's structure-function relationships and developing specific small molecule inhibitors, we have determined the solution structure of an engineered subdomain 2 of the NS3 RNA helicase of HCV, d(2Delta)-HCVh, and studied the backbone dynamics of this protein by (15)N-relaxation experiments using a model-free approach. The NMR studies on this 142-residue construct reveal that overall subdomain 2 of the HCV helicase is globular and well structured in solution even in the absence of the remaining parts of the NS3 protein. Its solution structure is very similar to the corresponding parts in the X-ray structures of the HCV NS3 helicase domain and intact bifunctional HCV NS3 protein. Slow hydrogen-deuterium exchange rates map to a well-structured, stable hydrophobic core region away from the subdomain interfaces. In contrast, the regions facing the subdomain interfaces in the HCV NS3 helicase domain are less well structured in d(2Delta)-HCVh, show fast hydrogen-deuterium exchange rates, and the analysis of the dynamic properties of d(2Delta)-HCVh reveals that these regions of the protein show distinct dynamical features. In particular, residues in motif V, which may be involved in transducing allosteric effects of nucleotide binding and hydrolysis on RNA binding, exhibit slow conformational exchange on the milli- to microsecond time-scale. The intrinsic conformational flexibility of this loop region may facilitate conformational changes required for helicase function.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11846566}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11846566 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11846566}}
==About this Structure==
==About this Structure==
-
1ONB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONB OCA].
+
1ONB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hepatitis_c_virus Hepatitis c virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONB OCA].
==Reference==
==Reference==
Line 28: Line 32:
[[Category: Wyss, D F.]]
[[Category: Wyss, D F.]]
[[Category: Alpha-beta-alpha]]
[[Category: Alpha-beta-alpha]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:03:36 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:28:34 2008''

Revision as of 16:28, 27 July 2008

Image:1onb.png

Template:STRUCTURE 1onb

Solution structure of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase

Template:ABSTRACT PUBMED 11846566

About this Structure

1ONB is a Single protein structure of sequence from Hepatitis c virus. Full experimental information is available from OCA.

Reference

Solution structure and backbone dynamics of an engineered arginine-rich subdomain 2 of the hepatitis C virus NS3 RNA helicase., Liu D, Wang YS, Gesell JJ, Wyss DF, J Mol Biol. 2001 Nov 30;314(3):543-61. PMID:11846566

Page seeded by OCA on Sun Jul 27 19:28:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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