1i16
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(New page: 200px<br /> <applet load="1i16" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i16" /> '''STRUCTURE OF INTERLEUKIN 16: IMPLICATIONS F...)
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Revision as of 15:18, 12 November 2007
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STRUCTURE OF INTERLEUKIN 16: IMPLICATIONS FOR FUNCTION, NMR, 20 STRUCTURES
Overview
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.
About this Structure
1I16 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site., Muhlhahn P, Zweckstetter M, Georgescu J, Ciosto C, Renner C, Lanzendorfer M, Lang K, Ambrosius D, Baier M, Kurth R, Holak TA, Nat Struct Biol. 1998 Aug;5(8):682-6. PMID:9699630
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