BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search
Home Forums Wiki NMR feeds Downloads Register Today's Posts



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
FANDAS
MestReS
V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
Gromacs
Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
 
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Old 05-07-2017, 04:20 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,777
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default The small GTPases Ras and Rheb studied by multidimensional NMR spectroscopy: structure and function.

The small GTPases Ras and Rheb studied by multidimensional NMR spectroscopy: structure and function.

The small GTPases Ras and Rheb studied by multidimensional NMR spectroscopy: structure and function.

Biol Chem. 2017 May 01;398(5-6):577-588

Authors: Schöpel M, Potheraveedu VN, Al-Harthy T, Abdel-Jalil R, Heumann R, Stoll R

Abstract
Ras GTPases are key players in cellular signalling because they act as binary switches. These states manifest through toggling between an active (GTP-loaded) and an inactive (GDP-loaded) form. The hydrolysis and replenishing of GTP is controlled by two additional protein classes: GAP (GTPase-activating)- and GEF (Guanine nucleotide exchange factors)-proteins. The complex interplay of the proteins is known as the GTPase-cycle. Several point mutations of the Ras protein deregulate this cycle. Mutations in Ras are associated with up to one-third of human cancers. The three isoforms of Ras (H, N, K) exhibit high sequence similarity and mainly differ in a region called HVR (hypervariable region). The HVR governs the differential action and cellular distribution of the three isoforms. Rheb is a Ras-like GTPase that is conserved from yeast to mammals. Rheb is mainly involved in activation of cell growth through stimulation of mTORC1 activity. In this review, we summarise multidimensional NMR studies on Rheb and Ras carried out to characterise their structure-function relationship and explain how the activity of these small GTPases can be modulated by low molecular weight compounds. These might help to design GTPase-selective antagonists for treatment of cancer and brain disease.


PMID: 28475102 [PubMed - in process]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Membrane interactions in small fast-tumbling bicelles as studied by (31)P NMR.
Membrane interactions in small fast-tumbling bicelles as studied by (31)P NMR. Membrane interactions in small fast-tumbling bicelles as studied by (31)P NMR. Biochim Biophys Acta. 2014 Dec 9; Authors: Bodor A, Kövér KE, Mäler L Abstract Small fast-tumbling bicelles are ideal for studies of membrane interactions at molecular level; they allow analysis of lipid properties using solution-state NMR. In the present study we used (31)P NMR relaxation to obtain detailed information on lipid head-group dynamics. We explored the effect...
nmrlearner Journal club 0 12-17-2014 09:43 PM
[NMR paper] A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues.
A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues. Angew Chem Int Ed Engl. 2013 Aug 22; Authors: Long D, Marshall CB, Bouvignies G, Mazhab-Jafari MT, Smith MJ, Ikura M, Kay LE Abstract ...
nmrlearner Journal club 0 09-17-2013 11:36 PM
Structure and function of G protein-coupled receptors using NMR spectroscopy
Structure and function of G protein-coupled receptors using NMR spectroscopy Publication year: 2010 Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 57, Issue 2</br> Joseph A. Goncalves, Shivani Ahuja, Sina Erfani, Markus Eilers, Steven O. Smith</br> </br> </br></br>
nmrlearner Journal club 0 03-09-2012 09:16 AM
Preparation of protein samples for NMR structure, function, and small-molecule screening studies.
Preparation of protein samples for NMR structure, function, and small-molecule screening studies. Preparation of protein samples for NMR structure, function, and small-molecule screening studies. Methods Enzymol. 2011;493:21-60 Authors: Acton TB, Xiao R, Anderson S, Aramini J, Buchwald WA, Ciccosanti C, Conover K, Everett J, Hamilton K, Huang YJ, Janjua H, Kornhaber G, Lau J, Lee DY, Liu G, Maglaqui M, Ma L, Mao L, Patel D, Rossi P, Sahdev S, Shastry R, Swapna GV, Tang Y, Tong S, Wang D, Wang H, Zhao L, Montelione GT In this chapter, we...
nmrlearner Journal club 0 03-05-2011 01:02 PM
[NMR paper] Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of
Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor. Related Articles Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor. Toxicol Lett. 1995 Dec;82-83:577-89 Authors: Hsu VL, Jia X, Kearns DR The solution structure of a type II DNA-binding protein (DBPII), transcription factor 1 (TF1), has been determined using NMR spectroscopy. A multidimensional, heteronuclear strategy was employed to overcome assignment ambiguities due to...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] Structure-function relationships in human epidermal growth factor studied by site-dir
Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR. Related Articles Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR. Biochemistry. 1991 Sep 10;30(36):8891-8 Authors: Hommel U, Dudgeon TJ, Fallon A, Edwards RM, Campbell ID In order to elucidate the mechanism of interaction between human epidermal growth factor (EGF) and its receptor, selected variants of EGF, differing by single amino acid substitutions, have been...
nmrlearner Journal club 0 08-21-2010 11:12 PM
[NMR paper] Structure-function relationships in human epidermal growth factor studied by site-dir
Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR. Related Articles Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR. Biochemistry. 1991 Sep 10;30(36):8891-8 Authors: Hommel U, Dudgeon TJ, Fallon A, Edwards RM, Campbell ID In order to elucidate the mechanism of interaction between human epidermal growth factor (EGF) and its receptor, selected variants of EGF, differing by single amino acid substitutions, have been...
nmrlearner Journal club 0 08-21-2010 11:12 PM
Structure and function of G protein-coupled receptors using NMR spectroscopy
Structure and function of G protein-coupled receptors using NMR spectroscopy Publication year: 2010 Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 12 May 2010</br> Joseph A., Goncalves , Shivani, Ahuja , Sina, Erfani , Markus, Eilers , Steven O., Smith</br> More...
nmrlearner Journal club 0 08-16-2010 03:50 AM



Posting Rules
You may not post new threads
You may not post replies
You may not post attachments
You may not edit your posts

BB code is On
Smilies are On
[IMG] code is On
HTML code is On
Trackbacks are Off
Pingbacks are Off
Refbacks are Off



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 04:47 PM.


Map