A View into the Blind Spot: Solution NMR Provides New Insights into Signal Transduction Across the Lipid Bilayer.

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A View into the Blind Spot: Solution NMR Provides New Insights into Signal Transduction Across the Lipid Bilayer.

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

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:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

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:

Isotope labeling:

Solid-state NMR:

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12-08-2010, 06:21 PM

nmrlearner

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A View into the Blind Spot: Solution NMR Provides New Insights into Signal Transduction Across the Lipid Bilayer.

A View into the Blind Spot: Solution NMR Provides New Insights into Signal Transduction Across the Lipid Bilayer.

Related Articles A View into the Blind Spot: Solution NMR Provides New Insights into Signal Transduction Across the Lipid Bilayer.

Structure. 2010 Dec 8;18(12):1559-1569

Authors: Call ME, Chou JJ

One of the most fundamental problems in cell biology concerns how cells communicate with their surroundings through surface receptors. The last few decades have seen major advances in understanding the mechanisms of receptor-ligand recognition and the biochemical consequences of such encounters. This review describes the emergence of solution nuclear magnetic resonance (NMR) spectroscopy as a powerful tool for the structural characterization of membrane-associated protein domains involved in transmembrane signaling. We highlight particularly instructive examples from the fields of immunoreceptor biology, growth hormone signaling, and cell adhesion. These signaling complexes comprise multiple subunits each spanning the membrane with a single helical segment that links extracellular ligand-binding domains to the cell interior. The apparent simplicity of this domain organization belies the complexity involved in cooperative assembly of functional structures that translate information across the cellular boundary.

PMID: 21134635 [PubMed - as supplied by publisher]

Source: PubMed

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