2f5h: Difference between revisions
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[[Image:2f5h.gif|left|200px]] | [[Image:2f5h.gif|left|200px]] | ||
'''Solution structure of the alpha-domain of human Metallothionein-3''' | {{Structure | ||
|PDB= 2f5h |SIZE=350|CAPTION= <scene name='initialview01'>2f5h</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Solution structure of the alpha-domain of human Metallothionein-3''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2F5H is a [ | 2F5H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F5H OCA]. | ||
==Reference== | ==Reference== | ||
Solution structure and dynamics of human metallothionein-3 (MT-3)., Wang H, Zhang Q, Cai B, Li H, Sze KH, Huang ZX, Wu HM, Sun H, FEBS Lett. 2006 Feb 6;580(3):795-800. Epub 2006 Jan 9. PMID:[http:// | Solution structure and dynamics of human metallothionein-3 (MT-3)., Wang H, Zhang Q, Cai B, Li H, Sze KH, Huang ZX, Wu HM, Sun H, FEBS Lett. 2006 Feb 6;580(3):795-800. Epub 2006 Jan 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16413543 16413543] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cadmium-thiolate cluster]] | [[Category: cadmium-thiolate cluster]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:48:19 2008'' | ||
Revision as of 17:48, 20 March 2008
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Solution structure of the alpha-domain of human Metallothionein-3
OverviewOverview
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.
About this StructureAbout this Structure
2F5H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure and dynamics of human metallothionein-3 (MT-3)., Wang H, Zhang Q, Cai B, Li H, Sze KH, Huang ZX, Wu HM, Sun H, FEBS Lett. 2006 Feb 6;580(3):795-800. Epub 2006 Jan 9. PMID:16413543
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