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Updated: Mar 13, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

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The C-terminal domain of TPX2 is made of alpha-helical tandem repeats

Luis Sanchez-Pulido1, Laurent Perez2,3, Steffen Kuhn4

  • 1MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, The University of Edinburgh, Western General Hospital, Crewe Road, Edinburgh, EH4 2XU, UK.

BMC Structural Biology
|October 27, 2016
PubMed
Abstract

Insights

Targeting Protein for Xklp2 (TPX2) has a conserved C-terminal domain forming a flexible alpha-helical solenoid crucial for microtubule nucleation. This study reveals its structure and evolutionary conservation across diverse species.

Area of Science:

  • Cell Biology
  • Structural Biology
  • Evolutionary Biology

Background:

  • Targeting Protein for Xklp2 (TPX2) is vital for spindle assembly and microtubule nucleation.
  • Existing knowledge on TPX2 protein family structure is limited, with few defined domains.
  • Previous studies identified TPX2 homologs in Chordata and plants.

Purpose of the Study:

  • To computationally and biophysically analyze the TPX2 protein family.
  • To elucidate the structure and evolutionary conservation of TPX2 proteins.
  • To provide insights for future structural investigations of TPX2.

Main Methods:

  • Computational sequence analyses and structural predictions.
  • Circular Dichroism (CD) measurements.
  • Molecular modeling.

Main Results:

  • The conserved C-terminal domain of TPX2, responsible for microtubule nucleation, comprises tandem repeats forming a flexible alpha-helical solenoid.
  • Predominant alpha-helical content was predicted and confirmed by CD measurements.
  • Homologs were identified in fungi and Diptera, with distinct domain organization in the latter.

Conclusions:

  • This study presents the first integrated computational and biophysical analysis of the TPX2 protein family.
  • The findings enhance understanding of TPX2 structure, function, and evolution.
  • The results guide future structural studies on this conserved protein family.
Keywords:
Alpha-solenoidCircular DichroismProtein sequence analysisProtein sequence tandem repeatsProtein structure predictionTPX2

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