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Updated: Jun 16, 2026

Examining BCL-2 Family Function with Large Unilamellar Vesicles
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Published on: October 5, 2012

A charge-sensitive loop in the FKBP38 catalytic domain modulates Bcl-2 binding

Mitcheell Maestre-Martínez1, Katja Haupt, Frank Edlich

  • 1Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle (Saale), Germany.

Journal of Molecular Recognition : JMR
|February 9, 2010
PubMed
Summary

Researchers discovered a new calcium-binding site in FKBP38, a regulator of Bcl-2. This site, involving electrostatic interactions, influences FKBP38

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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.