NMR paper NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop bin

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[NMR paper] NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop bin

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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:

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SAVES2 or SAVES4

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FANDAS

MestReS

V-NMR

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Backbone S2

Methyl S2

B-factor

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Gromacs

Amber

Antechamber

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Shiftx2

Sparta+

Camshift

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ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

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Protein disorder:

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11-24-2010, 08:49 PM

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NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop bin

NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop binding protein.

Related Articles NMR structure and dynamics of the RNA-binding site for the histone mRNA stem-loop binding protein.

RNA. 2002 Jan;8(1):83-96

Authors: DeJong ES, Marzluff WF, Nikonowicz EP

The 3' end of replication-dependent histone mRNAs terminate in a conserved sequence containing a stem-loop. This 26-nt sequence is the binding site for a protein, stem-loop binding protein (SLBP), that is involved in multiple aspects of histone mRNA metabolism and regulation. We have determined the structure of the 26-nt sequence by multidimensional NMR spectroscopy. There is a 16-nt stem-loop motif, with a conserved 6-bp stem and a 4-nt loop. The loop is closed by a conserved U.A base pair that terminates the canonical A-form stem. The pyrimidine-rich 4-nt loop, UUUC, is well organized with the three uridines stacking on the helix, and the fourth base extending across the major groove into the solvent. The flanking nucleotides at the base of the hairpin stem do not assume a unique conformation, despite the fact that the 5' flanking nucleotides are a critical component of the SLBP binding site.

PMID: 11871662 [PubMed - indexed for MEDLINE]

Source: PubMed

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