2f5h: Difference between revisions
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|PDB= 2f5h |SIZE=350|CAPTION= <scene name='initialview01'>2f5h</scene> | |PDB= 2f5h |SIZE=350|CAPTION= <scene name='initialview01'>2f5h</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f5h OCA], [http://www.ebi.ac.uk/pdbsum/2f5h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f5h RCSB]</span> | |||
}} | }} | ||
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[[Category: Wu, H M.]] | [[Category: Wu, H M.]] | ||
[[Category: Zhang, Q.]] | [[Category: Zhang, Q.]] | ||
[[Category: alpha helix]] | [[Category: alpha helix]] | ||
[[Category: cadmium-thiolate cluster]] | [[Category: cadmium-thiolate cluster]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:58:11 2008'' | ||
Revision as of 02:58, 31 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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