Peptide binding proclivities of calcium loaded calbindin-D28k.

Journal Article (Journal Article)

Calbindin-D28k is known to function as a calcium-buffering protein in the cell. Moreover, recent evidence shows that it also plays a role as a sensor. Using circular dichroism and NMR, we show that calbindin-D28k undergoes significant conformational changes upon binding calcium, whereas only minor changes occur when binding target peptides in its Ca(2+)-loaded state. NMR experiments also identify residues that undergo chemical shift changes as a result of peptide binding. The subsequent use of computational protein-protein docking protocols produce a model describing the interaction interface between calbindin-D28k and its target peptides.

Full Text

Duke Authors

Cited Authors

  • Kordys, DR; Bobay, BG; Thompson, RJ; Venters, RA; Cavanagh, J

Published Date

  • October 2, 2007

Published In

Volume / Issue

  • 581 / 24

Start / End Page

  • 4778 - 4782

PubMed ID

  • 17880944

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/j.febslet.2007.09.004

Language

  • eng

Conference Location

  • England