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      A vertebrate globin expressed in the brain.

      Nature
      Amino Acid Sequence, Animals, Brain, metabolism, Chromosome Mapping, Chromosomes, Human, Pair 14, Cloning, Molecular, Exons, Expressed Sequence Tags, Gene Expression Profiling, Globins, biosynthesis, classification, genetics, isolation & purification, Humans, Introns, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Nerve Tissue Proteins, Oxygen, Recombinant Fusion Proteins, Sequence Homology, Amino Acid

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          Abstract

          Haemoglobins and myoglobins constitute related protein families that function in oxygen transport and storage in humans and other vertebrates. Here we report the identification of a third globin type in man and mouse. This protein is predominantly expressed in the brain, and therefore we have called it neuroglobin. Mouse neuroglobin is a monomer with a high oxygen affinity (half saturation pressure, P50 approximately 2 torr). Analogous to myoglobin, neuroglobin may increase the availability of oxygen to brain tissue. The human neuroglobin gene (NGB), located on chromosome 14q24, has a unique exon-intron structure. Neuroglobin represents a distinct protein family that diverged early in metazoan evolution, probably before the Protostomia/Deuterostomia split.

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          Most cited references17

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          dbEST--database for "expressed sequence tags".

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            [6] Use of T7 RNA polymerase to direct expression of cloned genes

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              Correlation of DNA exonic regions with protein structural units in haemoglobin.

              P Go (1981)
              The discovery of intervening sequences (introns) in DNA led Gilbert and Tonegawa to suggest that a new protein could have been produced by bringing together certain segments of pre-existing ones. However, Blake argued that if DNA was so organized that coding sequences (exons) correspond to structural as well as functional units of proteins, then combinations would be much more likely to yield a stable globular conformation through being 'sums of parts'. In immunoglobulin heavy chain, four separate exons encode four different units, all with distinct functions and three of which have clear domain structures. However, in haemoglobin, which has no obvious domain structure, no clear conformational characteristics have so far been recognized for the segments encoded by exons. From a close inspection of their conformations by drawing various stereodiagrams and the Calpha-Calpha distance map, I now propose a conformational characterization of the segments as structural units.
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