1hib

<table><tr><td colspan='2'>[[1hib]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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='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>

[[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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== Publication Abstract from PubMed ==

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.

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:8364024<ref>PMID:8364024</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1hib" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Berman, H M]]

[[Category: Camacho, N P]]

[[Category: Goldman, A]]

[[Category: Green, D]]

[[Category: Schneider, B]]

[[Category: Smith, D R]]

[[Category: Young, P R]]

[[Category: Cytokine]]