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.


1ejo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ejo.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ejo.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ejo| PDB=1ejo | SCENE= }}
{{STRUCTURE_1ejo| PDB=1ejo | SCENE= }}
-
'''FAB FRAGMENT OF NEUTRALISING MONOCLONAL ANTIBODY 4C4 COMPLEXED WITH G-H LOOP FROM FMDV.'''
+
===FAB FRAGMENT OF NEUTRALISING MONOCLONAL ANTIBODY 4C4 COMPLEXED WITH G-H LOOP FROM FMDV.===
-
==Overview==
+
<!--
-
The crystal structure of a 15 amino acid synthetic peptide, corresponding to the sequence of the major antigenic site A (G-H loop of VP1) from a multiple variant of foot-and-mouth disease virus (FMDV), has been determined at 2.3 A resolution. The variant peptide includes four amino acid substitutions in the loop relative to the previously studied peptide representing FMDV C-S8c1 and corresponds to the loop of a natural FMDV isolate of subtype C(1). The peptide was complexed with the Fab fragment of the neutralizing monoclonal antibody 4C4. The peptide adopts a compact fold with a nearly cyclic conformation and a disposition of the receptor-recognition motif Arg-Gly-Asp that is closely related to the previously determined structure for the viral loop, as part of the virion, and for unsubstituted synthetic peptide antigen bound to neutralizing antibodies. New structural findings include the observation that well-defined solvent molecules appear to play a major role in stabilizing the conformation of the peptide and its interactions with the antibody. Structural results are supported by molecular-dynamic simulations. The multiply substituted peptide developed compensatory mechanisms to bind the antibody with a conformation very similar to that of its unsubstituted counterpart. One water molecule, which for steric reasons could not occupy the same position in the unsubstituted antigen, establishes hydrogen bonds with three peptide amino acids. The constancy of the structure of an antigenic domain despite multiple amino acid substitutions has implications for vaccine design.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10811933}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10811933 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10811933}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: G-h loop of vp1.]]
[[Category: G-h loop of vp1.]]
[[Category: Rgd motif]]
[[Category: Rgd motif]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:11:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:51:25 2008''

Revision as of 21:51, 30 June 2008

Image:1ejo.png

Template:STRUCTURE 1ejo

FAB FRAGMENT OF NEUTRALISING MONOCLONAL ANTIBODY 4C4 COMPLEXED WITH G-H LOOP FROM FMDV.

Template:ABSTRACT PUBMED 10811933

About this Structure

1EJO is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

A multiply substituted G-H loop from foot-and-mouth disease virus in complex with a neutralizing antibody: a role for water molecules., Ochoa WF, Kalko SG, Mateu MG, Gomes P, Andreu D, Domingo E, Fita I, Verdaguer N, J Gen Virol. 2000 Jun;81(Pt 6):1495-505. PMID:10811933

Page seeded by OCA on Tue Jul 1 00:51:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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