1hib
From Proteopedia
(New page: 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 /> | + | [[Image:1hib.gif|left|200px]]<br /><applet load="1hib" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hib" size=" | + | |
caption="1hib, resolution 2.4Å" /> | caption="1hib, resolution 2.4Å" /> | ||
'''THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION'''<br /> | '''THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Site-specific mutagenesis was used to obtain the human interleukin-1 beta | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1HIB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Berman, H | + | [[Category: Berman, H M.]] |
| - | [[Category: Camacho, N | + | [[Category: Camacho, N P.]] |
[[Category: Goldman, A.]] | [[Category: Goldman, A.]] | ||
[[Category: Green, D.]] | [[Category: Green, D.]] | ||
[[Category: Schneider, B.]] | [[Category: Schneider, B.]] | ||
| - | [[Category: Smith, D | + | [[Category: Smith, D R.]] |
| - | [[Category: Young, P | + | [[Category: Young, P R.]] |
[[Category: cytokine]] | [[Category: cytokine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:32 2008'' |
Revision as of 11:01, 21 February 2008
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THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION
Contents |
Overview
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.
Disease
Known disease associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147720]
About this Structure
1HIB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
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:8364024
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