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



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  
Unread 08-22-2010, 03:33 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,587
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 Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential R

Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence.

Related Articles Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence.

EMBO J. 1994 Mar 15;13(6):1270-9

Authors: Yang YS, Garbay C, Duchesne M, Cornille F, Jullian N, Fromage N, Tocque B, Roques BP

Src homology 3 (SH3) domains are found in numerous cytoplasmic proteins involved in intracellular signal transduction. We used 2-D 1H NMR to determine the structure of the SH3 domain of the guanosine triphosphatase-activating protein (GAP), an essential component of the Ras signaling pathway. The structure of the GAP SH3 domain (275-350) was found to be a compact beta-barrel made of six antiparallel beta-strands arranged in two roughly perpendicular beta-sheets with the acidic residues located at the surface of the protein. The Trp317, Trp319, Thr321 and Leu323 residues belonging to the sequence (317-326), which was shown to be essential for Ras signaling, formed two nearby lipophilic bulges followed by a hydrophilic domain (Arg324-Asp326). These structural data could be used to characterize the still unidentified downstream components of GAP, which are involved in Ras signaling, and to rationally design inhibitors of this pathway.

PMID: 8137811 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly. Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly. J Struct Funct Genomics. 2011 Sep 9; Authors: Yang Y, Ramelot TA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA Abstract ...
nmrlearner Journal club 0 09-10-2011 06:51 PM
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity. NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity. J Biol Chem. 2011 May 3; Authors: Shin J, Chakraborty G, Bharatham N, Kang C, Tochio N, Koshiba S, Kigawa T, Kim W, Kim KT, Yoon HS Vaccinia-related kinase 1 (VRK1) is one of the mitotic kinases which play important roles in cell cycle, nuclear condensation and transcription regulation. Kinase...
nmrlearner Journal club 0 05-06-2011 12:02 PM
Erratum to: NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6
Erratum to: NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6 Erratum to: NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6 Content Type Journal Article Pages 1-1 DOI 10.1007/s10858-011-9476-6 Authors
nmrlearner Journal club 0 02-23-2011 11:21 PM
Erratum to: NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6
Erratum to: NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6 Erratum to: NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6 Content Type Journal Article Pages 1-1 DOI 10.1007/s10858-011-9476-6 Authors
nmrlearner Journal club 0 02-23-2011 11:18 PM
NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6. J Biomol NMR. 2010 Aug;47(4):283-8 Authors: Chen J, Li Q, Liu CC, Zhou B, Bu G, Wang J
nmrlearner Journal club 0 09-24-2010 03:50 AM
[NMR paper] Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential R
Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence. EMBO J. 1994 Mar 15;13(6):1270-9 Authors: Yang YS, Garbay C, Duchesne M, Cornille F, Jullian N, Fromage N, Tocque B, Roques BP Src homology 3 (SH3) domains are found in numerous...
nmrlearner Journal club 0 08-22-2010 03:33 AM
[NMR paper] On deriving spatial protein structure from NMR or X-ray diffraction data.
On deriving spatial protein structure from NMR or X-ray diffraction data. Related Articles On deriving spatial protein structure from NMR or X-ray diffraction data. Ciba Found Symp. 1991;161:150-9; discussion 159-66 Authors: van Gunsteren WF, Gros P, Torda AE, Berendsen HJ, van Schaik RC During the last decade it has become possible to derive the spatial structure of small proteins in solution using multidimensional NMR spectroscopy measurements and interpreting the data in terms of a chemical atomic model. The NMR experiments generate a set...
nmrlearner Journal club 0 08-21-2010 11:16 PM
NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6 Content Type Journal Article DOI 10.1007/s10858-010-9426-8 Authors Jianglei Chen, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA Qianqian Li, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA Chia-Chen Liu, Washington University Departments of Pediatrics, and Cell Biology and Physiology, School of Medicine St. Louis MO 63110 USA
nmrlearner Journal club 0 08-14-2010 04:19 AM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This Thread:

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 - 2017, 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 02:38 AM.


Map