1I16

STRUCTURE OF INTERLEUKIN 16: IMPLICATIONS FOR FUNCTION, NMR, 20 STRUCTURES

Summary for 1I16

• Entry DOI: 10.2210/pdb1i16/pdb
• Descriptor: INTERLEUKIN 16 (1 entity in total)
• Functional Keywords: cytokine, lymphocyte chemoattractant factor, pdz domain
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 13394.90

Authors

Muehlhahn, P.,Zweckstetter, M.,Georgescu, J.,Ciosto, C.,Renner, C.,Lanzendoerfer, M.,Lang, K.,Ambrosius, D.,Baier, M.,Kurth, R.,Holak, T.A. (deposition date: 1998-05-20, release date: 1999-05-25, Last modification date: 2024-05-22)

Primary citation

Muhlhahn, P.,Zweckstetter, M.,Georgescu, J.,Ciosto, C.,Renner, C.,Lanzendorfer, M.,Lang, K.,Ambrosius, D.,Baier, M.,Kurth, R.,Holak, T.A.
Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site.
Nat.Struct.Biol., 5:682-686, 1998

PubMed 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.

PubMed: 9699630
DOI: 10.1038/1376

Experimental method

SOLUTION NMR