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PDBsum entry 2f5h
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Metal binding protein
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PDB id
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2f5h
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References listed in PDB file
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Key reference
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Title
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Solution structure and dynamics of human metallothionein-3 (mt-3).
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Authors
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H.Wang,
Q.Zhang,
B.Cai,
H.Li,
K.H.Sze,
Z.X.Huang,
H.M.Wu,
H.Sun.
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Ref.
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FEBS Lett, 2006,
580,
795-800.
[DOI no: ]
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PubMed id
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Abstract
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Alzheimer's disease is characterized by progressive loss of neurons accompanied
by the formation of intraneural neurofibrillary tangles and extracellular
amyloid plaques. Human neuronal growth inhibitory factor, classified as
metallothionein-3 (MT-3), was found to be related to the neurotrophic activity
promoting cortical neuron survival and dendrite outgrowth in the cell culture
studies. We have determined the solution structure of the alpha-domain of human
MT-3 (residues 32-68) by multinuclear and multidimensional NMR spectroscopy in
combination with the molecular dynamic simulated annealing approach. The human
MT-3 shows two metal-thiolate clusters, one in the N-terminus (beta-domain) and
one in the C-terminus (alpha-domain). The overall fold of the alpha-domain is
similar to that of mouse MT-3. However, human MT-3 has a longer loop in the
acidic hexapeptide insertion than that of mouse MT-3. Surprisingly, the backbone
dynamics of the protein revealed that the beta-domain exhibits similar internal
motion to the alpha-domain, although the N-terminal residues are more flexible.
Our results may provide useful information for understanding the
structure-function relationship of human MT-3.
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Figure 5.
Fig. 5. The 600 MHz two-dimensional ^1H–^15N HSQC
spectrum of ^15N-labeled human Cd[7]-MT-3 in 15 mM phosphate, pH
7.3, 298 K. The assignments are indicated by residue number and
one-letter amino acid code.
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Figure 6.
Fig. 6. Solution structure of the α-domain of human MT-3.
NMR solution structure ensembles (residues Cys34-Cys51 and
Glu62-Gln68) generated by superimposing the backbone coordinates
of the 10 best-converged structures (Upper). Ribbon diagram of
the mean structure of α-domain of human MT-3 showing a short
α-helices (Lower). Cd^2+ ions are highlighted in purple balls,
and their corresponding ^113Cd resonances are labeled in Fig. 2.
The atomic coordinates have been deposited in the Protein Data
Bank (PDBID: 2F5H).
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
FEBS Lett
(2006,
580,
795-800)
copyright 2006.
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