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1t4q

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[[Image:1t4q.jpg|left|200px]]
 
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{{Structure
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==Interleukin 1 beta F101W==
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|PDB= 1t4q |SIZE=350|CAPTION= <scene name='initialview01'>1t4q</scene>, resolution 2.1&Aring;
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<StructureSection load='1t4q' size='340' side='right'caption='[[1t4q]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1t4q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T4Q FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE= IL1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t4q OCA], [https://pdbe.org/1t4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t4q RCSB], [https://www.ebi.ac.uk/pdbsum/1t4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t4q ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1s0l|1S0L]], [[9ilb|9ILB]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t4q OCA], [http://www.ebi.ac.uk/pdbsum/1t4q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t4q RCSB]</span>
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[https://www.uniprot.org/uniprot/IL1B_HUMAN IL1B_HUMAN] Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.<ref>PMID:3920526</ref>
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}}
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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/t4/1t4q_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/main_output.php?pdb_ID=1t4q ConSurf].
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<div style="clear:both"></div>
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'''Interleukin 1 beta F101W'''
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==See Also==
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*[[Interleukin 3D structures|Interleukin 3D structures]]
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== References ==
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==Overview==
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<references/>
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The structural and energetic consequences of modifications to the hydrophobic cavity of interleukin 1-beta (IL-1beta) are described. Previous reports demonstrated that the entirely hydrophobic cavity of IL-1beta contains positionally disordered water. To gain a better understanding of the nature of this cavity and the water therein, a number of mutant proteins were constructed by site-directed mutagenesis, designed to result in altered hydrophobicity of the cavity. These mutations involve the replacement of specific phenylalanine residues, which circumscribe the cavity, with tyrosine, tryptophan, leucine and isoleucine. Using differential scanning calorimetry to determine the relative stabilities of the wild-type and mutant proteins, we found all of the mutants to be destabilizing. X-ray crystallography was used to identify the structural consequences of the mutations. No clear correlation between the hydrophobicities of the specific side-chains introduced and the resulting stabilities was found.
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__TOC__
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</StructureSection>
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==Disease==
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Known disease associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147720 147720]]
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==About this Structure==
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1T4Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4Q OCA].
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==Reference==
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Structural and energetic consequences of mutations in a solvated hydrophobic cavity., Adamek DH, Guerrero L, Blaber M, Caspar DL, J Mol Biol. 2005 Feb 11;346(1):307-18. Epub 2004 Dec 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15663946 15663946]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Adamek, D H.]]
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[[Category: Adamek DH]]
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[[Category: Caspar, D L.]]
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[[Category: Caspar DL]]
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[[Category: Guerrero, L.]]
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[[Category: Guerrero L]]
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[[Category: hydration cavity]]
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[[Category: il-1b]]
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[[Category: il1b]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:51:16 2008''
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Current revision

Interleukin 1 beta F101W

PDB ID 1t4q

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