2f5h
From Proteopedia
(New page: 200px<br /> <applet load="2f5h" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f5h" /> '''Solution structure of the alpha-domain of h...) |
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| - | [[Image:2f5h.gif|left|200px]]<br /> | + | [[Image:2f5h.gif|left|200px]]<br /><applet load="2f5h" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution structure of the alpha-domain of human Metallothionein-3'''<br /> | '''Solution structure of the alpha-domain of human Metallothionein-3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Alzheimer's disease is characterized by progressive loss of neurons | + | 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 Structure== | ==About this Structure== | ||
| - | 2F5H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2F5H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F5H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cai, B.]] | [[Category: Cai, B.]] | ||
| - | [[Category: Huang, Z | + | [[Category: Huang, Z X.]] |
| - | [[Category: Li, H | + | [[Category: Li, H Y.]] |
| - | [[Category: Sun, H | + | [[Category: Sun, H Z.]] |
| - | [[Category: Sze, K | + | [[Category: Sze, K H.]] |
[[Category: Wang, H.]] | [[Category: Wang, H.]] | ||
| - | [[Category: Wu, H | + | [[Category: Wu, H M.]] |
[[Category: Zhang, Q.]] | [[Category: Zhang, Q.]] | ||
[[Category: CD]] | [[Category: CD]] | ||
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[[Category: cadmium-thiolate cluster]] | [[Category: cadmium-thiolate cluster]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:17:55 2008'' |
Revision as of 15:18, 21 February 2008
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Solution structure of the alpha-domain of human Metallothionein-3
Overview
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 Structure
2F5H is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
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:16413543
Page seeded by OCA on Thu Feb 21 17:17:55 2008
Categories: Homo sapiens | Single protein | Cai, B. | Huang, Z X. | Li, H Y. | Sun, H Z. | Sze, K H. | Wang, H. | Wu, H M. | Zhang, Q. | CD | Alpha helix | Cadmium-thiolate cluster
