2f5h
From Proteopedia
|
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 CD 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 Mon Nov 12 21:59:45 2007
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
