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 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.
Max Planck Institute for Biochemistry, Martinsried, F.R.G., Germany.
P
P
Mühlhahn
M
M
Zweckstetter
J
J
Georgescu
C
C
Ciosto
C
C
Renner
M
M
Lanzendörfer
K
K
Lang
D
D
Ambrosius
M
M
Baier
R
R
Kurth
T A
TA
Holak
D000595:Amino Acid Sequence; D001665:Binding Sites; D003198:Computer Simulation; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D019410:Interleukin-16 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D009842:Oligopeptides / Q000378:metabolism*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D019410:Interleukin-16; D009842:Oligopeptides; D011994:Recombinant Proteins