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.


2qrz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2qrz.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2qrz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2qrz| PDB=2qrz | SCENE= }}
{{STRUCTURE_2qrz| PDB=2qrz | SCENE= }}
-
'''Cdc42 bound to GMP-PCP: Induced Fit by Effector is Required'''
+
===Cdc42 bound to GMP-PCP: Induced Fit by Effector is Required===
-
==Overview==
+
<!--
-
GTP-binding (G) proteins regulate the flow of information in cellular signaling pathways by alternating between a GTP-bound "active" state and a GDP-bound "inactive" state. Cdc42, a member of the Rho family of Ras-related small G-proteins, plays key roles in the regulation of cell shape, motility, and growth. Here we describe the high resolution x-ray crystal structure for Cdc42 bound to the GTP analog guanylyl beta,gamma-methylene-diphosphonate (GMP-PCP) (i.e. the presumed signaling-active state) and show that it is virtually identical to the structures for the signaling-inactive, GDP-bound form of the protein, contrary to what has been reported for Ras and other G-proteins. Especially surprising was that the GMP-PCP- and GDP-bound forms of Cdc42 did not show detectable differences in their Switch I and Switch II loops. Fluorescence studies using a Cdc42 mutant in which a tryptophan residue was introduced at position 32 of Switch I also showed that there was little difference in the Switch I conformation between the GDP- and GMP-PCP-bound states (i.e. &lt;10%), which again differed from Ras where much larger changes in Trp-32 fluorescence were observed when comparing these two nucleotide-bound states (&gt;30%). However, the binding of an effector protein induced significant changes in the Trp-32 emission specifically from GMP-PCP-bound Cdc42, as well as in the phosphate resonances for GTP bound to this G-protein as indicated in NMR studies. An examination of the available structures for Cdc42 complexed to different effector proteins, versus the x-ray crystal structure for GMP-PCP-bound Cdc42, provides a possible explanation for how effectors can distinguish between the GTP- and GDP-bound forms of this G-protein and ensure that the necessary conformational changes for signal propagation occur.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18348980}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18348980 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18348980}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Nucleotide-binding]]
[[Category: Nucleotide-binding]]
[[Category: Prenylation]]
[[Category: Prenylation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:33:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:24:32 2008''

Revision as of 19:24, 27 July 2008

Image:2qrz.png

Template:STRUCTURE 2qrz

Cdc42 bound to GMP-PCP: Induced Fit by Effector is Required

Template:ABSTRACT PUBMED 18348980

About this Structure

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

Reference

Effector Proteins Exert an Important Influence on the Signaling-active State of the Small GTPase Cdc42., Phillips MJ, Calero G, Chan B, Ramachandran S, Cerione RA, J Biol Chem. 2008 May 16;283(20):14153-64. Epub 2008 Mar 18. PMID:18348980

Page seeded by OCA on Sun Jul 27 22:24:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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