Structural alignment and analysis of two distantly related proteins: Aplysia limacina myoglobin and sea lamprey globin

Annalisa Pastore, Arthur M. Lesk, Martino Bolognesi, Silvia Onesti

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

Two new globin structures have recently been determined at high resolution: the globin from the mollusc Aplysia limacina at 1.6 A resolution and a new refinement of the structure from sea lamprey. Two amino acid sequences of these homologous molecules have only 30% residue identity in an optimal alignment. We discuss some of the problems arising in the alignment of Aplysia globin with other globins of known structure, a challenging problem because of the distant relationship. Four independent approaches were applied to the alignment of the Aplysia and lamprey globins, including those based on individual sequence comparisons, structural analysis, and the relatively new method of templates or fingerprints derived for an entire family of proteins. We also compare these two new structures with what is already known about the globin family. A detailed description of the two structures shows that the two molecules contain the main structural features common to all the globins so far studied with several minor but interesting hitherto unobserved variations.

Original languageEnglish (US)
Pages (from-to)240-250
Number of pages11
JournalProteins: Structure, Function, and Bioinformatics
Volume4
Issue number4
DOIs
StatePublished - 1988

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Structural alignment and analysis of two distantly related proteins: Aplysia limacina myoglobin and sea lamprey globin'. Together they form a unique fingerprint.

  • Cite this