1hib: Difference between revisions

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New page: left|200px<br /> <applet load="1hib" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hib, resolution 2.4Å" /> '''THE STRUCTURE OF AN ...
 
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[[Image:1hib.gif|left|200px]]<br />
<applet load="1hib" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hib, resolution 2.4&Aring;" />
'''THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION'''<br />


==Overview==
==THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION==
Site-specific mutagenesis was used to obtain the human interleukin-1 beta, mutant protein with glycine substituted for threonine at position 9 (IL-1, beta Thr9Gly). The mutant maintains receptor binding but exhibits, significantly reduced biological activity. The crystal structure of IL-1, beta Thr9Gly has been determined at 2.4-A resolution by molecular, replacement techniques and refined to a crystallographic R-factor of, 19.0%. IL-1 beta Thr9Gly crystallizes in a different space group (P6(5)22), than does native IL-1 beta (P4(3)); thus the molecules pack differently., Their overall structure is similar, nevertheless, with both composed of, 153 amino acids which form 12 antiparallel beta-strands. However, significant conformational differences both close to and far from the site, of the mutation may explain the mutant's altered properties.
<StructureSection load='1hib' size='340' side='right'caption='[[1hib]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hib]] 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=1HIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HIB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=1hib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hib OCA], [https://pdbe.org/1hib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hib RCSB], [https://www.ebi.ac.uk/pdbsum/1hib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hib ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== 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/hi/1hib_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=1hib ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
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]]
*[[Interleukin 3D structures|Interleukin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1HIB 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=1HIB OCA].
__TOC__
 
</StructureSection>
==Reference==
Structure of an interleukin-1 beta mutant with reduced bioactivity shows multiple subtle changes in conformation that affect protein-protein recognition., Camacho NP, Smith DR, Goldman A, Schneider B, Green D, Young PR, Berman HM, Biochemistry. 1993 Aug 31;32(34):8749-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8364024 8364024]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berman, H.M.]]
[[Category: Berman HM]]
[[Category: Camacho, N.P.]]
[[Category: Camacho NP]]
[[Category: Goldman, A.]]
[[Category: Goldman A]]
[[Category: Green, D.]]
[[Category: Green D]]
[[Category: Schneider, B.]]
[[Category: Schneider B]]
[[Category: Smith, D.R.]]
[[Category: Smith DR]]
[[Category: Young, P.R.]]
[[Category: Young PR]]
[[Category: cytokine]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:18:25 2007''

Latest revision as of 07:27, 7 February 2024

THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION

1hib, resolution 2.40Å

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