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Related Experiment Videos

Intramolecular signaling upon complexation

L W Guddat1, L Shan, Z C Fan

  • 1Harrington Cancer Center, Amarillo, Texas 79106.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|January 1, 1995
PubMed
Summary

Changes in crystal habits reveal protein conformational shifts. Ligand binding to Fab fragments induces significant structural alterations, impacting antibody effector functions.

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Area of Science:

  • Structural biology
  • Protein crystallography
  • Immunochemistry

Background:

  • Crystal habits serve as indicators of protein conformational changes.
  • Hemoglobin's conversion from unliganded to oxygenated form demonstrates this principle.

Purpose of the Study:

  • To investigate ligand-induced conformational changes in Fab fragments using X-ray crystallography.
  • To characterize structural alterations in the NC6.8 Fab fragment upon hapten binding.

Main Methods:

  • X-ray crystallography was employed to examine native and liganded Fab (NC6.8) forms.
  • Analysis of crystal habits (platy vs. prismatic) indicated structural transitions.

Main Results:

  • Hapten binding caused Fab crystals to disintegrate and reform, signifying structural changes.

Related Experiment Videos

  • Ligand complexation induced local and allosteric conformational changes, including light chain extension and heavy chain shortening.
  • The 'elbow bend' angle decreased by 31 degrees, and the constant domain pair shifted, displacing the heavy chain's carboxyl end by 19 Å.

    • Conclusions:

    • Ligand binding induces significant conformational flexibility in Fab fragments.
    • These allosteric changes may propagate to the Fc region, potentially influencing antibody effector functions like complement activation.