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.


1hql

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hql.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1hql.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hql| PDB=1hql | SCENE= }}
{{STRUCTURE_1hql| PDB=1hql | SCENE= }}
-
'''The xenograft antigen in complex with the B4 isolectin of Griffonia simplicifolia lectin-1'''
+
===The xenograft antigen in complex with the B4 isolectin of Griffonia simplicifolia lectin-1===
-
==Overview==
+
<!--
-
The shortage of organs for transplantation into human patients continues to be a driving force behind research into the use of tissues from non-human donors, particularly pig. The primary barrier to such xenotransplantation is the reaction between natural antibodies present in humans and Old World monkeys and the Gal alpha(1-3)Gal epitope (xenograft antigen, xenoantigen) found on the cell surfaces of the donor organ. This hyperacute immune response leads ultimately to graft rejection. Because of its high specificity for the xenograft antigen, isolectin 1-B(4) from Griffonia simplicifolia (GS-1-B(4)) has been used as an immunodiagnostic reagent. Furthermore, haptens that inhibit natural antibodies also inhibit GS-1-B(4) from binding to the xenoantigen. Here we report the first x-ray crystal structure of the xenograft antigen bound to a protein (GS-1-B(4)). The three-dimensional structure was determined from orthorhombic crystals at a resolution of 2.3 A. To probe the influence of binding on ligand properties, we report also the results of molecular dynamics (MD) simulations on this complex as well as on the free ligand. The MD simulations were performed with the AMBER force-field for proteins augmented with the GLYCAM parameters for glycosides and glycoproteins. The simulations were performed for up to 10 ns in the presence of explicit solvent. Through comparison with MD simulations performed for the free ligand, it has been determined that GS-1-B(4) recognizes the lowest energy conformation of the disaccharide. In addition, the x-ray and modeling data provide clear explanations for the reported specificities of the GS-1-B(4) lectin. It is anticipated that a further understanding of the interactions involving the xenograft antigen will help in the development of therapeutic agents for application in the prevention of hyperacute xenograft rejection.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11714721}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11714721 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11714721}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Lectin]]
[[Category: Lectin]]
[[Category: Xenograft antigen]]
[[Category: Xenograft antigen]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:07:49 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:32:48 2008''

Revision as of 05:32, 1 July 2008

Image:1hql.png

Template:STRUCTURE 1hql

The xenograft antigen in complex with the B4 isolectin of Griffonia simplicifolia lectin-1

Template:ABSTRACT PUBMED 11714721

About this Structure

Full crystallographic information is available from OCA.

Reference

The xenograft antigen bound to Griffonia simplicifolia lectin 1-B(4). X-ray crystal structure of the complex and molecular dynamics characterization of the binding site., Tempel W, Tschampel S, Woods RJ, J Biol Chem. 2002 Feb 22;277(8):6615-21. Epub 2001 Nov 19. PMID:11714721

Page seeded by OCA on Tue Jul 1 08:32:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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