NMR paper Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV

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[NMR paper] Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV

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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

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RDCs:

Pseudocontact shifts:

Protein geomtery:

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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Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

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MAXOCC

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08-21-2010, 04:03 PM

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Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV

Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.

Related Articles Solid-state NMR evidence for an antibody-dependent conformation of the V3 loop of HIV-1 gp120.

Nat Struct Biol. 1999 Feb;6(2):141-5

Authors: Weliky DP, Bennett AE, Zvi A, Anglister J, Steinbach PJ, Tycko R

Solid-state NMR measurements have been carried out on frozen solutions of the complex of a 24-residue peptide derived from the third variable (V3) loop of the HIV-1 envelope glycoprotein gp120 bound to the Fab fragment of an anti-gp120 antibody. The measurements place strong constraints on the conformation of the conserved central GPGR motif of the V3 loop in the antibody-bound state. In combination with earlier crystal structures of V3 peptide-antibody complexes and existing data on the cross-reactivity of the antibodies, the solid-state NMR measurements suggest that the Gly-Pro-Gly-Arg (GPGR) motif adopts an antibody-dependent conformation in the bound state and may be conformationally heterogeneous in unbound, full-length gp120. These measurements are the first application of solid-state NMR methods in a structural study of a peptide-protein complex.

PMID: 10048925 [PubMed - indexed for MEDLINE]

Source: PubMed

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