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

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 th...

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Veröffentlicht in:Nature structural & molecular biology 1998-08, Vol.5 (8), p.682-686
Hauptverfasser: Mühlhahn, P, Zweckstetter, M, Georgescu, J, Ciosto, C, Renner, C, Lanzendörfer, M, Lang, K, Ambrosius, D, Baier, M, Kurth, R, Holak, T A
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Sprache:eng
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Zusammenfassung: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.
ISSN:1072-8368
1545-9993
DOI:10.1038/1376