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Related Experiment Videos

Finding an average core structure: application to the globins

R B Altman1, M Gerstein

  • 1Section on Medical Informatics, Stanford University, CA 94305, USA.

Proceedings. International Conference on Intelligent Systems for Molecular Biology
|January 1, 1994
PubMed
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We developed a method to find structurally conserved regions in proteins. This analysis reveals distinct structural frameworks within the globin family, differentiating conserved cores from variable regions.

Area of Science:

  • Structural biology
  • Bioinformatics
  • Protein structure analysis

Background:

  • Proteins are essential biological molecules with diverse functions.
  • Understanding protein structure is crucial for deciphering their function and mechanisms.
  • Identifying conserved structural elements can provide insights into protein evolution and function.

Purpose of the Study:

  • To develop an automated procedure for identifying structurally conserved cores within aligned protein structures.
  • To apply this procedure to the globin protein family and analyze the identified structural core.
  • To investigate the relationship between structural variation and sequence conservation in proteins.

Main Methods:

  • Automated identification of structurally invariant atomic subsets (cores) from aligned protein structures.

Related Experiment Videos

  • Application of the procedure to the globin protein family.
  • Comparison of structural variation with sequence conservation.

    • Main Results:

    • The globin fold can be divided into a structurally variable region (heme-proximal residues, F, G, H helices) and a conserved structural framework (A, B, E, G, H helices).
    • The identified structural core shares similarities with the repressor protein framework.
    • Further partitions within the globin structural core may hold biological significance.
    • Structural core definition based on structural similarity does not always align with sequence conservation.

    Conclusions:

    • The developed procedure effectively identifies structurally conserved cores in protein families.
    • The globin fold exhibits a distinct structural framework with conserved and variable regions.
    • Structural and sequence conservation are not always directly correlated, highlighting the complexity of protein evolution.