Topological comparison of adenyl kinase with other proteins

Schulz, G. E.; Schirmer, R. Heiner

doi:10.1038/250142a0

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Topological comparison of adenyl kinase with other proteins

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Schulz, G. E.
Max Planck Institute for Medical Research, Max Planck Society;

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Schirmer, R. Heiner
Max Planck Institute for Medical Research, Max Planck Society;

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http://www.nature.com/nature/journal/v250/n5462/pdf/250142a0.pdf
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https://doi.org/10.1038/250142a0
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Citation

Schulz, G. E., & Schirmer, R. H. (1974). Topological comparison of adenyl kinase with other proteins. Nature, 250, 142-144. doi:10.1038/250142a0.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-DCA3-B

Abstract

A COMBINATION of amino acid sequence analysis1 and X-ray analysis has yielded the atomic structure of the enzyme adenyl kinase2 (adenylate kinase, EC 2.7.4.3). No protein of which the structure is known is so closely related to adenyl kinase that an amino acid sequence comparison3 or an exact geometrical comparison of the structures4–6 can be expected to indicate a relationship. Similarities with other proteins become apparent, however, if one restricts the comparison to topologies, that is, to chain folds without reference to the exact geometry. Since chain folds are particularly well conserved during evolution7 such a procedure might reveal distant relationships.