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Journal Article

Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site.

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Citation

Mühlhahn, P., Zweckstetter, M., Georgescu, J., Ciosto, C., Renner, C., Lanzendörfer, M., et al. (1998). Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site. Nature Structural and Molecular Biology, 5, 682-686. doi:10.1038/1376.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-A4A1-7
Abstract
The structure of a folded core of IL-16 is similar to that of intracellular protein modules called PDZ domains. IL-16 is thus the first extracellular protein found to have a PDZ-like fold. However, it does not exhibit normal peptide binding properties of PDZ domains. This is due to alterations of the structure at the 'PDZ-like binding site' of IL-16 (the GLGF cleft): the GLGF cleft of IL-16 is much smaller than those of PDZ-domains and is additionally blocked with a tryptophan side chain at its center. Our experiments indicate also that IL-16 nonspecifically aggregates in solution; but formation of a homo-tetrameric protein is not required, in contrast to previous suggestions, for its chemo-attractant activity.