1i16

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[[Image:1i16.png|left|200px]]
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==STRUCTURE OF INTERLEUKIN 16: IMPLICATIONS FOR FUNCTION, NMR, 20 STRUCTURES==
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<StructureSection load='1i16' size='340' side='right' caption='[[1i16]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1i16]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I16 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I16 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i16 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i16 RCSB], [http://www.ebi.ac.uk/pdbsum/1i16 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i1/1i16_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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{{STRUCTURE_1i16| PDB=1i16 | SCENE= }}
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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<ref>PMID:9699630</ref>
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===STRUCTURE OF INTERLEUKIN 16: IMPLICATIONS FOR FUNCTION, NMR, 20 STRUCTURES===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_9699630}}
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==About this Structure==
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[[1i16]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I16 OCA].
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==See Also==
==See Also==
*[[Interleukin|Interleukin]]
*[[Interleukin|Interleukin]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:009699630</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ambrosius, D.]]
[[Category: Ambrosius, D.]]

Revision as of 08:53, 28 September 2014

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

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