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.


1pz5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1pz5.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1pz5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1pz5| PDB=1pz5 | SCENE= }}
{{STRUCTURE_1pz5| PDB=1pz5 | SCENE= }}
-
'''Structural basis of peptide-carbohydrate mimicry in an antibody combining site'''
+
===Structural basis of peptide-carbohydrate mimicry in an antibody combining site===
-
==Overview==
+
<!--
-
The structure of a complex between the Fab fragment of the antibody (SYA/J6) specific for the cell surface O-antigen polysaccharide of the pathogen Shigella flexneri Y and an octapeptide (Met-Asp-Trp-Asn-Met-His-Ala-Ala), a functional mimic of the O-antigen, has been determined at 1.8-A resolution. Comparison of the structure with that of the complex with the pentasaccharide antigen [--&gt;2)-alpha-L-Rha-(1--&gt;2)-alpha-L-Rha-(1--&gt;3)-alpha-L-Rha-(1--&gt;3)-beta-D- GlcNAc-(1--&gt;2)-alpha-L-Rha-(1--&gt;] reveals the molecular recognition process by which a peptide mimics a carbohydrate in binding to an antibody. The binding modes of the two ligands differ considerably. Octapeptide binding complements the shape of the combining site groove much better than pentasaccharide binding. Moreover, the peptide makes a much greater number of contacts (126), which are mostly van der Waals interactions, with the Fab than the saccharide (74). An unusual feature is also the involvement of 12 water molecules in mediating hydrogen bonds between residues within the peptide or of the peptide and Fab. Despite better shape complementarity and greater number of contacts, the octapeptide binds with an affinity (KA = 2.5 x 10(5) M-1, measured by calorimetry) only approximately 2-fold tighter than the pentasaccharide. The structural results are relevant to the design of peptide mimetics with improved affinity for use as vaccines.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14645714}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14645714 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14645714}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Peptide-carbohydrate mimicry]]
[[Category: Peptide-carbohydrate mimicry]]
[[Category: Vaccine design]]
[[Category: Vaccine design]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:40:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:10:43 2008''

Revision as of 11:10, 29 July 2008

Image:1pz5.png

Template:STRUCTURE 1pz5

Structural basis of peptide-carbohydrate mimicry in an antibody combining site

Template:ABSTRACT PUBMED 14645714

About this Structure

Full crystallographic information is available from OCA.

Reference

Structural basis of peptide-carbohydrate mimicry in an antibody-combining site., Vyas NK, Vyas MN, Chervenak MC, Bundle DR, Pinto BM, Quiocho FA, Proc Natl Acad Sci U S A. 2003 Dec 9;100(25):15023-8. Epub 2003 Nov 25. PMID:14645714

Page seeded by OCA on Tue Jul 29 14:10:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pz5"
Personal tools