2F5H
Solution structure of the alpha-domain of human Metallothionein-3
Summary for 2F5H
| Entry DOI | 10.2210/pdb2f5h/pdb |
| Descriptor | Metallothionein-3, CADMIUM ION (2 entities in total) |
| Functional Keywords | alpha helix, cadmium-thiolate cluster, metal binding protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 4264.08 |
| Authors | |
| Primary citation | Wang, H.,Zhang, Q.,Cai, B.,Li, H.Y.,Sze, K.H.,Huang, Z.X.,Wu, H.M.,Sun, H.Z. Solution structure and dynamics of human metallothionein-3 (MT-3) Febs Lett., 580:795-800, 2006 Cited by PubMed Abstract: 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. PubMed: 16413543DOI: 10.1016/j.febslet.2005.12.099 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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