Source:http://linkedlifedata.com/resource/pubmed/id/16413543
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2006-1-31
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
580
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
795-800
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pubmed:dateRevised |
2010-4-12
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pubmed:meshHeading |
pubmed-meshheading:16413543-Alzheimer Disease,
pubmed-meshheading:16413543-Amyloid,
pubmed-meshheading:16413543-Animals,
pubmed-meshheading:16413543-Cell Survival,
pubmed-meshheading:16413543-Dendrites,
pubmed-meshheading:16413543-Humans,
pubmed-meshheading:16413543-Mice,
pubmed-meshheading:16413543-Nerve Tissue Proteins,
pubmed-meshheading:16413543-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:16413543-Protein Structure, Secondary,
pubmed-meshheading:16413543-Protein Structure, Tertiary,
pubmed-meshheading:16413543-Structure-Activity Relationship
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pubmed:year |
2006
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pubmed:articleTitle |
Solution structure and dynamics of human metallothionein-3 (MT-3).
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pubmed:affiliation |
Department of Chemistry and Open Laboratory of Chemical Biology, The University of Hong Kong, Pokfulam Road, Hong Kong, PR China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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