Literature DB >> 7463490

The relationship between coding sequences and function in some heme binding proteins.

P Argos, M G Rossmann.   

Abstract

It is known that globin genes contain three exons with the middle exon coding for a four-helical supersecondary structure responsible for heme binding. Since this portion of the globin peptide chain can be structurally superimposed onto the cytochrome c and cytochrome b5 chains (Argos and Rossmann 1979), it can be inferred that the cytochrome c gene will contain only one coding sequence while the cytochrome b5 gene will be composed of three exons as found in the globin gene.

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Year:  1980        PMID: 7463490     DOI: 10.1007/bf01731583

Source DB:  PubMed          Journal:  J Mol Evol        ISSN: 0022-2844            Impact factor:   2.395


  5 in total

1.  Structural comparisons of heme binding proteins.

Authors:  P Argos; M G Rossmann
Journal:  Biochemistry       Date:  1979-10-30       Impact factor: 3.162

2.  Why genes in pieces?

Authors:  W Gilbert
Journal:  Nature       Date:  1978-02-09       Impact factor: 49.962

3.  Exons encode protein functional units.

Authors:  C C Blake
Journal:  Nature       Date:  1979-02-22       Impact factor: 49.962

4.  The relationship between coding sequences and function in haemoglobin.

Authors:  W A Eaton
Journal:  Nature       Date:  1980-03-13       Impact factor: 49.962

5.  Comparison of total sequence of a cloned rabbit beta-globin gene and its flanking regions with a homologous mouse sequence.

Authors:  A van Ooyen; J van den Berg; N Mantei; C Weissmann
Journal:  Science       Date:  1979-10-19       Impact factor: 47.728

  5 in total

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