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.


1cc0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1cc0.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1cc0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cc0| PDB=1cc0 | SCENE= }}
{{STRUCTURE_1cc0| PDB=1cc0 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX'''
+
===CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX===
-
==Overview==
+
<!--
-
Like all Rho (Ras homology) GTPases, RhoA functions as a molecular switch in cell signaling, alternating between GTP- and GDP-bound states, with its biologically inactive GDP-bound form maintained as a cytosolic complex with RhoGDI (guanine nucleotide-exchange inhibitor). The crystal structures of RhoA-GDP and of the C-terminal immunoglobulin-like domain of RhoGDI (residues 67-203) are known, but the mechanism by which the two proteins interact is not known. The functional human RhoA-RhoGDI complex has been expressed in yeast and crystallized (P6(5)22, unit-cell parameters a = b = 139, c = 253 A, two complexes in the asymmetric unit). Although diffraction from these crystals extends to 3.5 A and is highly anisotropic, the experimentally phased (MAD plus MIR) electron-density map was adequate to reveal the mutual disposition of the two molecules. The result was validated by molecular-replacement calculations when data were corrected for anisotropy. Furthermore, the N-terminus of RhoGDI (the region involved in inhibition of nucleotide exchange) can be identified in the electron-density map: it is bound to the switch I and switch II regions of RhoA, occluding an epitope which binds Dbl-like nucleotide-exchange factors. The entrance of the hydrophobic pocket of RhoGDI is 25 A from the last residue in the RhoA model, with its C-terminus oriented to accommodate the geranylgeranyl group without conformational change in RhoA.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10489445}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10489445 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10489445}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: G-protein]]
[[Category: G-protein]]
[[Category: Rho gtpase]]
[[Category: Rho gtpase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:33:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:32:03 2008''

Revision as of 17:32, 30 June 2008

Image:1cc0.png

Template:STRUCTURE 1cc0

CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX

Template:ABSTRACT PUBMED 10489445

About this Structure

1CC0 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

How RhoGDI binds Rho., Longenecker K, Read P, Derewenda U, Dauter Z, Liu X, Garrard S, Walker L, Somlyo AV, Nakamoto RK, Somlyo AP, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 1999 Sep;55(Pt 9):1503-15. PMID:10489445

Page seeded by OCA on Mon Jun 30 20:32:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cc0"
Personal tools