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Structural and Functional Studies of the Neuronal Growth Inhibitory Factor, Human Metallothionein-3

Structural and Functional Studies of the Neuronal Growth Inhibitory Factor, Human Metallothionein-3


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This dissertation, "Structural and Functional Studies of the Neuronal Growth Inhibitory Factor, Human Metallothionein-3" by Hui, Wang, 王暉, was obtained from The University of Hong Kong (Pokfulam, Hong Kong) and is being sold pursuant to Creative Commons: Attribution 3.0 Hong Kong License. The content of this dissertation has not been altered in any way. We have altered the formatting in order to facilitate the ease of printing and reading of the dissertation. All rights not granted by the above license are retained by the author. Abstract: Abstract of thesis entitled STRUCTURAL AND FUNCTIONAL STUDIES OF THE NEURONAL GROWTH INHIBITORY FACTOR, HUMAN METALLOTHIONEIN-3 Submitted by WANG Hui for the degree of Doctor of Philosophy at The University of Hong Kong in August 2007 Alzheimer's disease (AD) is characterized by progressive loss of neurons accompanied by the formation of intraneural neurofibrillary tangles and extracellar amyloid plaques. The brain specific member of the metallothionein (MT) family, metallothionein-3 inhibits the growth and survival of neurons whose down-regulation can lead to the enhancement of neurotrophic activity in Alzheimer Disease's brain. Due to the distinct biological activity, MT-3 is also identified as a growth inhibitory factor (GIF). The solution structure of the α-domain of human MT-3 (residue 32-68) has been determined by multinuclear and multidimensional NMR spectroscopy in combination with the molecular dynamic simulated annealing approach. Human MT-3 shows two metal-thiolate clusters, the M Cys cluster in the N-terminus (β-domain) and the M Cys 3 9 4 11 cluster in the C-terminus (α-domain). The overall fold of the α-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 β-domain exhibits similar internal motion to the α-domain, although the N-terminal residues are more flexible. With additional residual dipolar couplings (RDCs), the structure refinements of the two domains were performed respectively. For the α-domain, after refinement, the overall fold is essentially identical to that obtained without such RDCs constraints only with a slight movement in the acidic loop towards the metal ions. On the other hand, for the β-domain, the additional two sets of RDCs make it possible to determine the structure of the flexible β-domain, and the refined structures of the β-domain showed a different 113 overall fold from other MTs. Furthermore, Cd NMR studies on the mutants P7SP9A- hMT-3 and C30S/∆33-35-hMT-3 revealed their different characteristics of the metal- thiolate clusters. It is known that nitric oxide (NO) has a pivotal role in zinc toxicity in neurons. The nitrosylation of thiols in metallothioneins (MTs), which is mediated by NO, possibly results in the 'somatic' zinc release by destroying the metal-thiolate clusters. By using 113 1 15 Cd and 2D [ H, N] HSQC NMR spectroscopy, the NO-induced metal release from human MT-3 was examined, and the structural changes associated with the interaction was monitored. The NMR technique allows the individual metal release from the protein and the associated structural changes of the protein at level of individual residue to be monitored. The exposure of human MT-3 to NO leads to a non-selective release of the three metals from the β-domain. In contrast to MT-1/2, two of the bound metals in the α- domain were also partially released with the domain structure remained almost unchanged. Further addition of NO resulted in complete release of metals and concomitant unfolding of the protein. The preference of metal release in the α-domain was attributed to the two different coordination environment for the four cadmium/zinc atoms. The results of the structural and biochemical studies may provide useful informa


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Product Details
  • ISBN-13: 9781361427781
  • Publisher: Open Dissertation Press
  • Publisher Imprint: Open Dissertation Press
  • Height: 279 mm
  • No of Pages: 230
  • Weight: 544 gr
  • ISBN-10: 1361427787
  • Publisher Date: 27 Jan 2017
  • Binding: Paperback
  • Language: English
  • Spine Width: 12 mm
  • Width: 216 mm


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