2F5H

Solution structure of the alpha-domain of human Metallothionein-3

2F5H の概要

• エントリーDOI: 10.2210/pdb2f5h/pdb
• 分子名称: Metallothionein-3, CADMIUM ION (2 entities in total)
• 機能のキーワード: alpha helix, cadmium-thiolate cluster, metal binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4264.08

構造登録者

Wang, H.,Zhang, Q.,Cai, B.,Li, H.Y.,Sze, K.H.,Huang, Z.X.,Wu, H.M.,Sun, H.Z. (登録日: 2005-11-25, 公開日: 2006-05-30, 最終更新日: 2024-05-29)

主引用文献

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

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: 16413543
DOI: 10.1016/j.febslet.2005.12.099

実験手法

SOLUTION NMR