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.


2it5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2it5.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2it5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2it5| PDB=2it5 | SCENE= }}
{{STRUCTURE_2it5| PDB=2it5 | SCENE= }}
-
'''Crystal Structure of DCSIGN-CRD with man6'''
+
===Crystal Structure of DCSIGN-CRD with man6===
-
==Overview==
+
<!--
-
The dendritic cell surface receptor DC-SIGN and the closely related endothelial cell receptor DC-SIGNR specifically recognize high mannose N-linked carbohydrates on viral pathogens. Previous studies have shown that these receptors bind the outer trimannose branch Manalpha1-3[Manalpha1-6]Manalpha present in high mannose structures. Although the trimannoside binds to DC-SIGN or DC-SIGNR more strongly than mannose, additional affinity enhancements are observed in the presence of one or more Manalpha1-2Manalpha moieties on the nonreducing termini of oligomannose structures. The molecular basis of this enhancement has been investigated by determining crystal structures of DC-SIGN bound to a synthetic six-mannose fragment of a high mannose N-linked oligosaccharide, Manalpha1-2Manalpha1-3[Manalpha1-2Manalpha1-6]Manalpha1-6Man and to the disaccharide Manalpha1-2Man. The structures reveal mixtures of two binding modes in each case. Each mode features typical C-type lectin binding at the principal Ca2+-binding site by one mannose residue. In addition, other sugar residues form contacts unique to each binding mode. These results suggest that the affinity enhancement displayed toward oligosaccharides decorated with the Manalpha1-2Manalpha structure is due in part to multiple binding modes at the primary Ca2+ site, which provide both additional contacts and a statistical (entropic) enhancement of binding.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17150970}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17150970 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17150970}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: C-type lectin]]
[[Category: C-type lectin]]
[[Category: Protein carbohydrate complex]]
[[Category: Protein carbohydrate complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:50:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:22:07 2008''

Revision as of 03:22, 29 July 2008

Image:2it5.png

Template:STRUCTURE 2it5

Crystal Structure of DCSIGN-CRD with man6

Template:ABSTRACT PUBMED 17150970

About this Structure

2IT5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Multiple modes of binding enhance the affinity of DC-SIGN for high mannose N-linked glycans found on viral glycoproteins., Feinberg H, Castelli R, Drickamer K, Seeberger PH, Weis WI, J Biol Chem. 2007 Feb 9;282(6):4202-9. Epub 2006 Dec 6. PMID:17150970

Page seeded by OCA on Tue Jul 29 06:22:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2it5"
Personal tools