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.


1sl4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sl4.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1sl4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sl4| PDB=1sl4 | SCENE= }}
{{STRUCTURE_1sl4| PDB=1sl4 | SCENE= }}
-
'''Crystal Structure of DC-SIGN carbohydrate recognition domain complexed with Man4'''
+
===Crystal Structure of DC-SIGN carbohydrate recognition domain complexed with Man4===
-
==Overview==
+
<!--
-
Both the dendritic cell receptor DC-SIGN and the closely related endothelial cell receptor DC-SIGNR bind human immunodeficiency virus and enhance infection. However, biochemical and structural comparison of these receptors now reveals that they have very different physiological functions. By screening an extensive glycan array, we demonstrated that DC-SIGN and DC-SIGNR have distinct ligand-binding properties. Our structural and mutagenesis data explain how both receptors bind high-mannose oligosaccharides on enveloped viruses and why only DC-SIGN binds blood group antigens, including those present on microorganisms. DC-SIGN mediates endocytosis, trafficking as a recycling receptor and releasing ligand at endosomal pH, whereas DC-SIGNR does not release ligand at low pH or mediate endocytosis. Thus, whereas DC-SIGN has dual ligand-binding properties and functions both in adhesion and in endocytosis of pathogens, DC-SIGNR binds a restricted set of ligands and has only the properties of an adhesion receptor.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15195147}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15195147 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15195147}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: C-type lectin]]
[[Category: C-type lectin]]
[[Category: Dc-sign]]
[[Category: Dc-sign]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:50:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:19:50 2008''

Revision as of 14:19, 27 July 2008

Image:1sl4.png

Template:STRUCTURE 1sl4

Crystal Structure of DC-SIGN carbohydrate recognition domain complexed with Man4

Template:ABSTRACT PUBMED 15195147

About this Structure

1SL4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR., Guo Y, Feinberg H, Conroy E, Mitchell DA, Alvarez R, Blixt O, Taylor ME, Weis WI, Drickamer K, Nat Struct Mol Biol. 2004 Jul;11(7):591-8. Epub 2004 Jun 13. PMID:15195147

Page seeded by OCA on Sun Jul 27 17:19:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sl4"
Personal tools