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

Mühlhahn, P., Zweckstetter, M., Georgescu, J., Ciosto, C., Renner, C., Lanzendörfer, M., et al. (1998). Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site. Nature Structural and Molecular Biology, 5, 682-686. doi:10.1038/1376.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-A4A1-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-A4B4-E
Genre: Journal Article

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2353571.pdf (Publisher version), 826KB
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 Creators:
Mühlhahn, P., Author
Zweckstetter, M.1, Author              
Georgescu, J., Author
Ciosto, C., Author
Renner, C., Author
Lanzendörfer, M., Author
Lang, K., Author
Ambrosius, D., Author
Baier, M., Author
Kurth, R., Author
Holak, T. A., Author
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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 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.

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Language(s): eng - English
 Dates: 1998-08
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/1376
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Title: Nature Structural and Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 5 Sequence Number: - Start / End Page: 682 - 686 Identifier: -