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PDBsum entry 1i16
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References listed in PDB file
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Key reference
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Title
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Structure of interleukin 16 resembles a pdz domain with an occluded peptide binding site.
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Authors
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P.Mühlhahn,
M.Zweckstetter,
J.Georgescu,
C.Ciosto,
C.Renner,
M.Lanzendörfer,
K.Lang,
D.Ambrosius,
M.Baier,
R.Kurth,
T.A.Holak.
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Ref.
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Nat Struct Biol, 1998,
5,
682-686.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1. a, Steady-state heteronuclear ^15N{^1 H}-NOE for the
backbone amides of IL-16. Residues for which no results are
shown correspond either to prolines or to residues for which the
relaxation data could not be extracted. b, ^1H-^15N HSQC
spectrum of human IL-16^1−130 at pH 7.4, circles identify
residues for which cross peaks were observed only at pH 6.5.
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Figure 4.
Figure 4. a, Comparison of the overall topologies of IL-16 and
Dlg_A. b, Conformation of the Gly-Leu-Gly-Phe cleft in human
IL-16 (red).The side chain of Trp 99 is marked in green.
Conformation of the side chain atoms for residues 41−46 are
also shown. Conformation of the GLGF site in human Dlg_A is in
blue^22. The side chain of Ala 529 is shown in green (this
residue corresponds to Trp 99 in IL-16).
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(1998,
5,
682-686)
copyright 1998.
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