NMR paper A model of the iron responsive element RNA hairpin loop structure determined from NMR

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[NMR paper] A model of the iron responsive element RNA hairpin loop structure determined from NMR

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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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08-22-2010, 02:20 PM

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A model of the iron responsive element RNA hairpin loop structure determined from NMR

A model of the iron responsive element RNA hairpin loop structure determined from NMR and thermodynamic data.

Related Articles A model of the iron responsive element RNA hairpin loop structure determined from NMR and thermodynamic data.

Biochemistry. 1996 Oct 22;35(42):13586-96

Authors: Laing LG, Hall KB

The iron responsive element (IRE) is a conserved RNA structure that is found in the 5' UTR of ferritin mRNA and in the 3' UTR of transferrin receptor mRNA. It is the binding site of the iron responsive protein (IRP), and the interaction is part of the regulation of cellular iron metabolism. The IRE six-nucleotide hairpin loop, 5'C1A2G3U4G5N6, is conserved in sequence, and mutations have shown that it is required for IRP binding. On the basis of the thermodynamic and NMR experiments utilized here, the IRE loop structure 5'C1A2G3U4G5C6, is described in detail. Measurements of loop stability show that it has 2.9 kcal/mol more free energy than predicted. NMR data suggest that there is hydrogen bonding between C1 and G5 in a tertiary interaction across the loop. A model structure, produced by MC-SYM/energy minimization, illustrates the conformational flexibility of U4 and C6, which appear to exhibit considerable local motion in solution. NMR data indicate that the position of G3 is not well defined, leading to two families of loop structures.

PMID: 8885838 [PubMed - indexed for MEDLINE]

Source: PubMed

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