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.


1cdu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1cdu.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1cdu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cdu| PDB=1cdu | SCENE= }}
{{STRUCTURE_1cdu| PDB=1cdu | SCENE= }}
-
'''STRUCTURE OF T-CELL SURFACE GLYCOPROTEIN CD4 MUTANT WITH PHE 43 REPLACED BY VAL'''
+
===STRUCTURE OF T-CELL SURFACE GLYCOPROTEIN CD4 MUTANT WITH PHE 43 REPLACED BY VAL===
-
==Overview==
+
<!--
-
The T-cell antigen coreceptor CD4 also serves as the receptor for the envelope glycoprotein gp120 of HIV. Extensive mutational analysis of CD4 has implicated residues from a portion of the extracellular amino-terminal domain (D1) in gp120 binding. However, none of these proteins has been fully characterized biophysically, and thus the precise effects on molecular structure and binding interactions are unknown. In the present study, we produced soluble versions of three mutant CD4 molecules (F43V, G47S, and A55F) and characterized their structural properties, thermostability, and ability to bind gp120. Crystallographic and thermodynamic analysis showed minimal structural alterations in the F43V and G47S mutant proteins, which have solvent-exposed mutant side chains. In contrast, some degree of disorder appears to exist in the folded state of A55F, as a result of mutating a buried side chain. Real time kinetic measurements of the interaction of the mutant proteins with gp120 showed affinity decreases of 5-fold for G47S, 50-fold for A55F, and 200-fold for F43V. Although both rate constants for the binding reaction were affected by these mutations, the loss in affinity was mainly due to a decrease in on rates, with less drastic changes occurring in the off rates. These observations suggest the involvement of conformational adaptation in the CD4-gp120 interaction. Together, the structural and kinetic data confirm that F43V is a critical residue in gp120 recognition site, which may also include main chain interactions at residue Gly-47.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8986758}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8986758 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8986758}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: T-cell surface glycoprotein]]
[[Category: T-cell surface glycoprotein]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:37:14 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:36:19 2008''

Revision as of 17:36, 30 June 2008

Image:1cdu.png

Template:STRUCTURE 1cdu

STRUCTURE OF T-CELL SURFACE GLYCOPROTEIN CD4 MUTANT WITH PHE 43 REPLACED BY VAL

Template:ABSTRACT PUBMED 8986758

About this Structure

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

Reference

Kinetic and structural analysis of mutant CD4 receptors that are defective in HIV gp120 binding., Wu H, Myszka DG, Tendian SW, Brouillette CG, Sweet RW, Chaiken IM, Hendrickson WA, Proc Natl Acad Sci U S A. 1996 Dec 24;93(26):15030-5. PMID:8986758

Page seeded by OCA on Mon Jun 30 20:36:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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