1i16

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==Overview==
==Overview==
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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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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==
==About this Structure==
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[[Category: Ciosto, C.]]
[[Category: Ciosto, C.]]
[[Category: Georgescu, J.]]
[[Category: Georgescu, J.]]
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[[Category: Holak, T.A.]]
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[[Category: Holak, T A.]]
[[Category: Kurth, R.]]
[[Category: Kurth, R.]]
[[Category: Lang, K.]]
[[Category: Lang, K.]]
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[[Category: pdz domain]]
[[Category: pdz domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:59:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:54 2008''

Revision as of 11:06, 21 February 2008


1i16

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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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