Crystallization and preliminary x-ray diffraction analysis of a novel mannose-binding lectin with antiretroviral properties from Polygonatum cyrtonema hua

Protein Pept Lett. 2008;15(4):411-4. doi: 10.2174/092986608784246551.

Abstract

A novel antiretroviral protein Polygonatum cyrtonema lectin (PCL) belonging to the monocot mannose-binding lectin (MMBL) superfamily has been crystallized using hanging-drop vapor-diffusion method. The crystals diffract to 2.0 A resolution and belong to space group P2(1), with unit-cell parameters of a=39.308 A, b=48.317 A, c=112.221 A, and beta=90.12 degrees . Preliminary analysis indicates that the asymmetric unit contains four PCL molecules with a solvent content of about 45%. A set of X-ray data has been collected for the crystal structure determination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-Retroviral Agents / chemistry*
  • Anti-Retroviral Agents / isolation & purification
  • Anti-Retroviral Agents / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Plant Lectins / chemistry*
  • Plant Lectins / isolation & purification
  • Plant Lectins / metabolism
  • Polygonatum / chemistry*
  • Sequence Alignment
  • X-Ray Diffraction

Substances

  • Anti-Retroviral Agents
  • Plant Lectins