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 11-22-2017, 02:01 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 18,077
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 Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.

Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.

Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.

Proc Natl Acad Sci U S A. 2017 Nov 20;:

Authors: Elkins MR, Williams JK, Gelenter MD, Dai P, Kwon B, Sergeyev IV, Pentelute BL, Hong M

Abstract
The influenza M2 protein not only forms a proton channel but also mediates membrane scission in a cholesterol-dependent manner to cause virus budding and release. The atomic interaction of cholesterol with M2, as with most eukaryotic membrane proteins, has long been elusive. We have now determined the cholesterol-binding site of the M2 protein in phospholipid bilayers using solid-state NMR spectroscopy. Chain-fluorinated cholesterol was used to measure cholesterol proximity to M2 while sterol-deuterated cholesterol was used to measure bound-cholesterol orientation in lipid bilayers. Carbon-fluorine distance measurements show that at a cholesterol concentration of 17 mol%, two cholesterol molecules bind each M2 tetramer. Cholesterol binds the C-terminal transmembrane (TM) residues, near an amphipathic helix, without requiring a cholesterol recognition sequence motif. Deuterium NMR spectra indicate that bound cholesterol is approximately parallel to the bilayer normal, with the rough face of the sterol rings apposed to methyl-rich TM residues. The distance- and orientation-restrained cholesterol-binding site structure shows that cholesterol is stabilized by hydrophobic interactions with the TM helix and polar and aromatic interactions with neighboring amphipathic helices. At the 1:2 binding stoichiometry, lipid (31)P spectra show an isotropic peak indicative of high membrane curvature. This M2-cholesterol complex structure, together with previously observed M2 localization at phase boundaries, suggests that cholesterol mediates M2 clustering to the neck of the budding virus to cause the necessary curvature for membrane scission. The solid-state NMR approach developed here is generally applicable for elucidating the structural basis of cholesterol's effects on membrane protein function.


PMID: 29158386 [PubMed - as supplied by publisher]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Ca(2+) ATPase conformational transitions in lipid bilayers mapped by site-directed ethylation and solid-state NMR.
Ca(2+) ATPase conformational transitions in lipid bilayers mapped by site-directed ethylation and solid-state NMR. Ca(2+) ATPase conformational transitions in lipid bilayers mapped by site-directed ethylation and solid-state NMR. ACS Chem Biol. 2015 Dec 9; Authors: Vostrikov VV, Gustavsson M, Gopinath T, Mullen D, Dicke AA, Truong V, Veglia G Abstract To transmit signals across cellular compartments, many membrane-embedded enzymes undergo extensive conformational rearrangements. Monitoring these events in lipid bilayers by...
nmrlearner Journal club 0 12-10-2015 05:49 PM
[NMR paper] Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy.
Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy. Related Articles Paramagnetic doping of a 7TM membrane protein in lipid bilayers by Gd(3+)-complexes for solid-state NMR spectroscopy. J Biomol NMR. 2013 Dec 4; Authors: Ullrich SJ, Hölper S, Glaubitz C Abstract A considerable limitation of NMR spectroscopy is its inherent low sensitivity. Approximately 90*% of the measuring time is used by the spin system to return to its Boltzmann equilibrium after excitation, which is...
nmrlearner Journal club 0 12-07-2013 01:00 PM
[NMR paper] Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy.
Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy. Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy. J Biomol NMR. 2013 Aug 21; Authors: Mote KR, Gopinath T, Veglia G Abstract The low sensitivity inherent to both the static and magic angle spinning techniques of solid-state NMR (ssNMR) spectroscopy...
nmrlearner Journal club 0 08-23-2013 01:07 AM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR. Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR. J Am Chem Soc. 2011 Mar 14; Authors: Yang J, Aslimovska L, Glaubitz C Environmental factors such as temperature, hydration, and lipid bilayer properties are tightly coupled to the dynamics of membrane proteins. So far, site-resolved data visualizing the protein's response to alterations in these factors are rare, and conclusions had to be drawn from dynamic data averaged over the whole protein...
nmrlearner Journal club 0 03-16-2011 04:15 PM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR Jun Yang, Lubica Aslimovska and Clemens Glaubitz http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109766n/aop/images/medium/ja-2010-09766n_0011.gif Journal of the American Chemical Society DOI: 10.1021/ja109766n http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/VmNlca5pCIw
nmrlearner Journal club 0 03-15-2011 05:56 AM
Specific Binding of Adamantane Drugs and Direction of Their Polar Amines in the Pore of the Influenza M2 Transmembrane Domain in Lipid Bilayers and Dodecylphosphocholine Micelles Determined by NMR Spectroscopy.
Specific Binding of Adamantane Drugs and Direction of Their Polar Amines in the Pore of the Influenza M2 Transmembrane Domain in Lipid Bilayers and Dodecylphosphocholine Micelles Determined by NMR Spectroscopy. Specific Binding of Adamantane Drugs and Direction of Their Polar Amines in the Pore of the Influenza M2 Transmembrane Domain in Lipid Bilayers and Dodecylphosphocholine Micelles Determined by NMR Spectroscopy. J Am Chem Soc. 2011 Mar 7; Authors: Cady SD, Wang J, Wu Y, Degrado WF, Hong M The transmembrane domain of the influenza M2...
nmrlearner Journal club 0 03-09-2011 02:20 PM
Specific Binding of Adamantane Drugs and Direction of Their Polar Amines in the Pore of the Influenza M2 Transmembrane Domain in Lipid Bilayers and Dodecylphosphocholine Micelles Determined by NMR Spectroscopy
Specific Binding of Adamantane Drugs and Direction of Their Polar Amines in the Pore of the Influenza M2 Transmembrane Domain in Lipid Bilayers and Dodecylphosphocholine Micelles Determined by NMR Spectroscopy Sarah D. Cady, Jun Wang, Yibing Wu, William F. DeGrado and Mei Hong http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja102581n/aop/images/medium/ja-2010-02581n_0011.gif Journal of the American Chemical Society DOI: 10.1021/ja102581n http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
nmrlearner Journal club 0 03-08-2011 04:02 AM
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR.
Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR. Lipid-Protein Correlations in Nanoscale Phospholipid Bilayers by Solid-State NMR. Biochemistry. 2010 Aug 30; Authors: Kijac A, Shih AY, Nieuwkoop AJ, Schulten K, Sligar SG, Rienstra CM Nanodiscs are an example of discoidal nanoscale lipid/protein particles that have been extremely useful for the biochemical and biophysical characterization of membrane proteins. They are discoidal lipid bilayer fragments encircled and stabilized by two amphipathic helical...
nmrlearner Journal club 0 09-02-2010 03:58 PM


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 11:13 AM.


Map