1i16

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

1i16 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IL16_HUMAN Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.^[1] ^[2] Isoform 1 may act as a scaffolding protein that anchors ion channels in the membrane.^[3] ^[4] Isoform 3 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.^[5] ^[6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Center DM, Cruikshank WW, Zhang Y. Nuclear pro-IL-16 regulation of T cell proliferation: p27(KIP1)-dependent G0/G1 arrest mediated by inhibition of Skp2 transcription. J Immunol. 2004 Feb 1;172(3):1654-60. PMID:14734747
↑ Zhang Y, Tuzova M, Xiao ZX, Cruikshank WW, Center DM. Pro-IL-16 recruits histone deacetylase 3 to the Skp2 core promoter through interaction with transcription factor GABP. J Immunol. 2008 Jan 1;180(1):402-8. PMID:18097041
↑ Center DM, Cruikshank WW, Zhang Y. Nuclear pro-IL-16 regulation of T cell proliferation: p27(KIP1)-dependent G0/G1 arrest mediated by inhibition of Skp2 transcription. J Immunol. 2004 Feb 1;172(3):1654-60. PMID:14734747
↑ Zhang Y, Tuzova M, Xiao ZX, Cruikshank WW, Center DM. Pro-IL-16 recruits histone deacetylase 3 to the Skp2 core promoter through interaction with transcription factor GABP. J Immunol. 2008 Jan 1;180(1):402-8. PMID:18097041
↑ Center DM, Cruikshank WW, Zhang Y. Nuclear pro-IL-16 regulation of T cell proliferation: p27(KIP1)-dependent G0/G1 arrest mediated by inhibition of Skp2 transcription. J Immunol. 2004 Feb 1;172(3):1654-60. PMID:14734747
↑ Zhang Y, Tuzova M, Xiao ZX, Cruikshank WW, Center DM. Pro-IL-16 recruits histone deacetylase 3 to the Skp2 core promoter through interaction with transcription factor GABP. J Immunol. 2008 Jan 1;180(1):402-8. PMID:18097041
↑ Muhlhahn P, Zweckstetter M, Georgescu J, Ciosto C, Renner C, Lanzendorfer M, Lang K, Ambrosius D, Baier M, Kurth R, Holak TA. Structure of interleukin 16 resembles a PDZ domain with an occluded peptide binding site. Nat Struct Biol. 1998 Aug;5(8):682-6. PMID:9699630 doi:10.1038/1376

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i16"

@@ Line 1: / Line 1: @@
-[[Image:1i16.gif|left|200px]]<br />
-<applet load="1i16" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1i16" />
-'''STRUCTURE OF INTERLEUKIN 16: IMPLICATIONS FOR FUNCTION, NMR, 20 STRUCTURES'''<br />
-==Overview==
+==STRUCTURE OF INTERLEUKIN 16: IMPLICATIONS FOR FUNCTION, NMR, 20 STRUCTURES==
-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.
+<StructureSection load='1i16' size='340' side='right'caption='[[1i16]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1i16]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1I16 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i16 OCA], [https://pdbe.org/1i16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i16 RCSB], [https://www.ebi.ac.uk/pdbsum/1i16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i16 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/IL16_HUMAN IL16_HUMAN] Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4.<ref>PMID:14734747</ref> <ref>PMID:18097041</ref>   Isoform 1 may act as a scaffolding protein that anchors ion channels in the membrane.<ref>PMID:14734747</ref> <ref>PMID:18097041</ref>   Isoform 3 is involved in cell cycle progression in T-cells. Appears to be involved in transcriptional regulation of SKP2 and is probably part of a transcriptional repression complex on the core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-binding subunit the GABP transcription factor complex) and HDAC3 thus maintaining transcriptional repression and blocking cell cycle progression in resting T-cells.<ref>PMID:14734747</ref> <ref>PMID:18097041</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i1/1i16_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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/main_output.php?pdb_ID=1i16 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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==
+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>
-I16 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I16 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9699630 9699630]
+</div>
-[[Category: Homo sapiens]]
+<div class="pdbe-citations 1i16" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
-[[Category: Ambrosius, D.]]
-[[Category: Baier, M.]]
-[[Category: Ciosto, C.]]
-[[Category: Georgescu, J.]]
-[[Category: Holak, T.A.]]
-[[Category: Kurth, R.]]
-[[Category: Lang, K.]]
-[[Category: Lanzendoerfer, M.]]
-[[Category: Muehlhahn, P.]]
-[[Category: Renner, C.]]
-[[Category: Zweckstetter, M.]]
-[[Category: cytokine]]
-[[Category: lymphocyte chemoattractant factor]]
-[[Category: pdz domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:25:06 2007''
+==See Also==
+*[[Interleukin 3D structures|Interleukin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Ambrosius D]]
+[[Category: Baier M]]
+[[Category: Ciosto C]]
+[[Category: Georgescu J]]
+[[Category: Holak TA]]
+[[Category: Kurth R]]
+[[Category: Lang K]]
+[[Category: Lanzendoerfer M]]
+[[Category: Muehlhahn P]]
+[[Category: Renner C]]
+[[Category: Zweckstetter M]]

1i16

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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