NMR paper The interaction of [13C]-enriched colchicine with tubulin as determined by NMR spectr

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[NMR paper] The interaction of [13C]-enriched colchicine with tubulin as determined by NMR spectr

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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:

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Amber

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Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

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Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

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RCI

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HADDOCK

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NOEs, other restraints:

Chemical shifts:

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FANDAS

MestReS

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B-factor

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PPM

CheShift-2- Cα

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Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

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NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

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08-21-2010, 11:12 PM

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The interaction of [13C]-enriched colchicine with tubulin as determined by NMR spectr

The interaction of [13C]-enriched colchicine with tubulin as determined by NMR spectroscopy.

Related Articles The interaction of [13C]-enriched colchicine with tubulin as determined by NMR spectroscopy.

Biochim Biophys Acta. 1991 Jul 12;1078(3):339-44

Authors: Osei AA, Everett GW, Ringel I, Himes RH

[13C]Colchicine, labeled at the tropolone ring methoxy carbon, was used to study interactions with tubulin containing either Mg2+ or Mn2+ at the high affinity divalent cation binding site. Similar experiments were carried out in the presence of excess free divalent cation. The results show that: (1) when Mn2+ occupies the N-site, the 13C signal of the colchicine methoxy carbon of protein-bound colchicine is not broadened, indicating that in protein-bound colchicine the tropolone methoxy group is not close to the N-site cation; (2) when excess Mn2+ is present in solution this 13C signal is severely broadened, indicating that a low affinity divalent cation site or the exchangeable site (E-site) divalent cation is situated near the colchicine binding site; and (3) in the absence of paramagnetic ions a downfield chemical shift is observed for the tropolone methoxy carbon of colchicine upon binding to tubulin, suggesting that colchicine binds near an aromatic group(s) on tubulin.

PMID: 1859824 [PubMed - indexed for MEDLINE]

Source: PubMed

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