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.


1k8r

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1k8r.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1k8r.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1k8r| PDB=1k8r | SCENE= }}
{{STRUCTURE_1k8r| PDB=1k8r | SCENE= }}
-
'''Crystal structure of Ras-Bry2RBD complex'''
+
===Crystal structure of Ras-Bry2RBD complex===
-
==Overview==
+
<!--
-
BACKGROUND: The small GTP binding protein Ras has important roles in cellular growth and differentiation. Mutant Ras is permanently active and contributes to cancer development. In its activated form, Ras interacts with effector proteins, frequently initiating a kinase cascade. In the lower eukaryotic Schizosaccharomyces pombe, Byr2 kinase represents a Ras target that in terms of signal-transduction hierarchy can be considered a homolog of mammalian Raf-kinase. The activation mechanism of protein kinases by Ras is not understood, and there is no detailed structural information about Ras binding domains (RBDs) in nonmammalian organisms. RESULTS: The crystal structure of the Ras-Byr2RBD complex at 3 A resolution shows a complex architecture similar to that observed in mammalian homologous systems, with an interprotein beta sheet stabilized by predominantly polar interactions between the interacting components. The C-terminal half of the Ras switch I region contains most of the contact anchors, while on the Byr2 side, a number of residues from topologically distinct regions are involved in complex stabilization. A C-terminal helical segment, which is not present in the known mammalian homologous systems and which is part of the auto-inhibitory region, has an additional binding site outside the switch I region. CONCLUSIONS: The structure of the Ras-Byr2 complex confirms the Ras binding module as a communication element mediating Ras-effector interactions; the Ras-Byr2 complex is also conserved in a lower eukaryotic system like yeast, which is in contrast to other small GTPase families. The extra helical segment might be involved in kinase activation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11709168}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11709168 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11709168}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Signal transduction]]
[[Category: Signal transduction]]
[[Category: Ubiquitin fold]]
[[Category: Ubiquitin fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:26:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 09:57:28 2008''

Revision as of 06:57, 2 July 2008

Image:1k8r.png

Template:STRUCTURE 1k8r

Crystal structure of Ras-Bry2RBD complex

Template:ABSTRACT PUBMED 11709168

About this Structure

1K8R is a Protein complex structure of sequences from Homo sapiens and Schizosaccharomyces pombe. Full crystallographic information is available from OCA.

Reference

The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast., Scheffzek K, Grunewald P, Wohlgemuth S, Kabsch W, Tu H, Wigler M, Wittinghofer A, Herrmann C, Structure. 2001 Nov;9(11):1043-50. PMID:11709168

Page seeded by OCA on Wed Jul 2 09:57:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k8r"
Personal tools