منابع مشابه
Preferential binding of copper to the beta domain of metallothionein.
Proteolytic studies of rat liver metallothionein reconstituted in vitro with Cu salts revealed that the 2 metal centers fill in an ordered fashion. The B cluster in the NH2-terminal beta domain fills prior to Cu binding in cluster A. This is in contradistinction to cluster formation induced by the binding of Cd or Zn ions in which cluster A is the center of initial binding. The formation of met...
متن کاملan outlook on the nature of mental creations after belonging to public domain
the public domain of copyright which considers the end of protection period, attempts to cause balance among the rights of authors, society and third parties. so at the end of financial rights of author’s protection period the possibility of free utilization of these literary works will be possible. but in this situation one of the controversial difficulties is the nature of these kinds of lite...
متن کاملAnti-metallothionein IgG and levels of metallothionein in autistic families.
Metallothioneins (MTs) are a family of small proteins containing 61-68 amino acids with an unusually high concentration of cysteine. MT-1, the most functional and active MT in humans, has the ability to react with and enhance the detoxification of a number of metals including zinc, mercury, copper and cadmium. MT dysfunction may result, then, in many of the aetiological syndromes observed in au...
متن کاملX-ray absorption studies of the copper-beta domain of rat liver metallothionein.
Rat liver metallothionein contains two domains, each of which enfolds a separate metal-thiolate cluster. The binding stoichiometry of these clusters depends on the particular metal ion bound. In the aminoterminal beta domain the cluster can accommodate either three Cd(II) ions or six Cu(I) ions. The Cd ions are known to be coordinated in a tetrahedral geometry. In order to better understand the...
متن کاملThe Nature of Protein Domain Evolution: Shaping the Interaction Network
The proteomes that make up the collection of proteins in contemporary organisms evolved through recombination and duplication of a limited set of domains. These protein domains are essentially the main components of globular proteins and are the most principal level at which protein function and protein interactions can be understood. An important aspect of domain evolution is their atomic stru...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)34802-6