NMR paper Determination of the three-dimensional structure of CC chemokine monocyte chemoattrac

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[NMR paper] Determination of the three-dimensional structure of CC chemokine monocyte chemoattrac

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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, 03:31 PM

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Determination of the three-dimensional structure of CC chemokine monocyte chemoattrac

Determination of the three-dimensional structure of CC chemokine monocyte chemoattractant protein 3 by 1H two-dimensional NMR spectroscopy.

Related Articles Determination of the three-dimensional structure of CC chemokine monocyte chemoattractant protein 3 by 1H two-dimensional NMR spectroscopy.

Biochemistry. 1997 Apr 15;36(15):4412-22

Authors: Meunier S, Bernassau JM, Guillemot JC, Ferrara P, Darbon H

MCP-3 is a beta chemokine consisting of 76 amino acid residues. It has been described to be involved in the activation of all leukocytic cells, activation mediated by the presence of multiple binding sites on the target cells. Its three-dimensional structure has been studied by making use of two-dimensional 1H NMR spectroscopy. MCP-3 exhibits the same monomeric structure as the other chemokines, i.e., a three-stranded antiparallel beta sheet covered on one face by an alpha helix. Although it belongs to the same subfamily as RANTES (Chung et al., 1995; Faitbrother et al., 1994) and hMIP-1beta (Lodi et al., 1994), the MCP-3 dimer is folded like IL-8 with the so-called alphabeta sandwich structural motif. Structural and sequence analysis gives clear indications suggesting that the other MCP chemokines may have the same quaternary structure, contrary to the other beta chemokines.

PMID: 9109648 [PubMed - indexed for MEDLINE]

Source: PubMed

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