Sandbox Reserved 556

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(New page: <!-- PLEASE DO NOT DELETE THIS TEMPLATE --> {{NCSU_BIOL414_Sandbox}} <!-- PLEASE ADD YOUR CONTENT BELOW HERE --> Hi everyone, Here is your very own Proteopedia Page to play with. This page...)
Current revision (17:32, 24 May 2012) (edit) (undo)
 
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{{NCSU_BIOL414_Sandbox}}
{{NCSU_BIOL414_Sandbox}}
<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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Hi everyone,
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Hi Jay,
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Here is your very own Proteopedia Page to play with.
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Here is your very own Proteopedia Page for pdb code: 3K8Y.
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This page is not publicly available yet,
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Your presentation is scheduled for: June 20.
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so don't worry about making mistakes that
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other people will see.
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Have Fun!
Have Fun!
Greg Buhrman
Greg Buhrman
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[[Image:3k8y.png|left|200px]]
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<!--
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The line below this paragraph, containing "STRUCTURE_3k8y", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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{{STRUCTURE_3k8y| PDB=3k8y | SCENE= }}
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===Allosteric modulation of H-Ras GTPase===
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<!--
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The line below this paragraph, {{ABSTRACT_PUBMED_20194776}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 20194776 is the PubMed ID number.
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{{ABSTRACT_PUBMED_20194776}}
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==About this Structure==
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3K8Y is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K8Y OCA].
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==Reference==
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<ref group="xtra">PMID:20194776</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
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[[Category: Buhrman, G.]]
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[[Category: Holzapfel, G.]]
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[[Category: Mattos, C.]]
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[[Category: Acetylation]]
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[[Category: Cell membrane]]
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[[Category: Disease mutation]]
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[[Category: Golgi apparatus]]
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[[Category: Gtp-binding]]
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[[Category: Lipoprotein]]
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[[Category: Membrane]]
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[[Category: Methylation]]
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[[Category: Nucleotide-binding]]
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[[Category: Oncoprotein]]
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[[Category: Palmitate]]
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[[Category: Prenylation]]
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[[Category: Protein-nucleotide complex]]
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[[Category: Proto-oncogene]]
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[[Category: S-nitrosylation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 12 10:34:56 2010''

Current revision

This Sandbox is Reserved from 05/22/2012, through 07/22/2012 for use in the course "BIOL 414" taught by Greg Buhrman at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 551 through Sandbox Reserved 590.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Hi Jay, Here is your very own Proteopedia Page for pdb code: 3K8Y. Your presentation is scheduled for: June 20.

Have Fun!

Greg Buhrman


PDB ID 3k8y

Drag the structure with the mouse to rotate
3k8y, resolution 1.30Å ()
Ligands: , , ,
Gene: HRAS, HRAS1 (Homo sapiens)
Related: 2rge, 3k9n, 3k9l
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Allosteric modulation of H-Ras GTPase

Publication Abstract from PubMed

Ras and its effector Raf are key mediators of the Ras/Raf/MEK/ERK signal transduction pathway. Mutants of residue Q61 impair the GTPase activity of Ras and are found prominently in human cancers. Yet the mechanism through which Q61 contributes to catalysis has been elusive. It is thought to position the catalytic water molecule for nucleophilic attack on the gamma-phosphate of GTP. However, we previously solved the structure of Ras from crystals with symmetry of the space group R32 in which switch II is disordered and found that the catalytic water molecule is present. Here we present a structure of wild-type Ras with calcium acetate from the crystallization mother liquor bound at a site remote from the active site and likely near the membrane. This results in a shift in helix 3/loop 7 and a network of H-bonding interactions that propagates across the molecule, culminating in the ordering of switch II and placement of Q61 in the active site in a previously unobserved conformation. This structure suggests a direct catalytic role for Q61 where it interacts with a water molecule that bridges one of the gamma-phosphate oxygen atoms to the hydroxyl group of Y32 to stabilize the transition state of the hydrolysis reaction. We propose that Raf together with the binding of Ca(2+) and a negatively charged group mimicked in our structure by the acetate molecule induces the ordering of switch I and switch II to complete the active site of Ras.

Allosteric modulation of Ras positions Q61 for a direct role in catalysis., Buhrman G, Holzapfel G, Fetics S, Mattos C, Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):4931-6. Epub 2010 Mar 1. PMID:20194776

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3K8Y is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Buhrman G, Holzapfel G, Fetics S, Mattos C. Allosteric modulation of Ras positions Q61 for a direct role in catalysis. Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):4931-6. Epub 2010 Mar 1. PMID:20194776

Page seeded by OCA on Wed May 12 10:34:56 2010

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