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Nat Struct Biol. 1998 Aug;5(8):682-6.

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

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1
Max Planck Institute for Biochemistry, Martinsried, F.R.G., Germany.

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.

PMID:
9699630
DOI:
10.1038/1376
[Indexed for MEDLINE]
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