We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1iud

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1iud.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1iud.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1iud| PDB=1iud | SCENE= }}
{{STRUCTURE_1iud| PDB=1iud | SCENE= }}
-
'''MALTODEXTRIN-BINDING PROTEIN INSERTION/DELETION MUTANT WITH AN INSERTED B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS'''
+
===MALTODEXTRIN-BINDING PROTEIN INSERTION/DELETION MUTANT WITH AN INSERTED B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS===
-
==Overview==
+
<!--
-
We report the crystal structure of MalE-B133, a recombinant form of the maltodextrin-binding protein (MBP) of Escherichia coli carrying an inserted amino-acid sequence of a B-cell epitope from the preS2 region of the hepatitis B virus (HBV). The structure was determined by molecular replacement methods and refined to 2.7 A resolution. MalE-B133 is an insertion/deletion mutant of MBP in which residues from positions 134 to 142, an external alpha helix in the wild-type structure, are replaced by a foreign peptide segment of 19 amino acids. The inserted residues correspond to the preS2 sequence from positions 132 to 145 and five flanking residues that arise from the creation of restriction sites. The conformation of the recombinant protein, excluding the inserted segment, closely resembles that of wild-type MBP in the closed maltose-bound form. MalE-B133 was shown by previous studies to display certain immunogenic and antigenic properties of the hepatitis B surface antigen (HBsAg), which contains the preS2 region. The crystal structure reveals the conformation of the first nine epitope residues (preS2 positions 132 to 140) exposed on the surface of the molecule. The remaining five epitope residues (preS2 positions 141 to 145) are not visible in electron density maps. The path of the polypeptide chain in the visible portion of the insert differs from that of the deleted segment in the structure of wild-type MBP, displaying a helical conformation at positions 134 to 140 (preS2 sequence numbering). A tripeptide (Asp-Pro-Arg) at the N terminus of the helix forms a stable structural motif that may be implicated in the cross-reactivity of anti-HBsAg antibodies with the hybrid protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9037707}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9037707 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9037707}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Sugar transport]]
[[Category: Sugar transport]]
[[Category: Viral epitope insertion]]
[[Category: Viral epitope insertion]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:25:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:01:07 2008''

Revision as of 11:01, 1 July 2008

Image:1iud.png

Template:STRUCTURE 1iud

MALTODEXTRIN-BINDING PROTEIN INSERTION/DELETION MUTANT WITH AN INSERTED B-CELL EPITOPE FROM THE PRES2 REGION OF HEPATITIS B VIRUS

Template:ABSTRACT PUBMED 9037707

About this Structure

1IUD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of a recombinant form of the maltodextrin-binding protein carrying an inserted sequence of a B-cell epitope from the preS2 region of hepatitis B virus., Saul FA, Vulliez-le Normand B, Lema F, Bentley GA, Proteins. 1997 Jan;27(1):1-8. PMID:9037707

Page seeded by OCA on Tue Jul 1 14:01:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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