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 />
[[Image:1hib.gif|left|200px]]<br /><applet load="1hib" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1hib" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1hib, resolution 2.4&Aring;" />
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 />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HIB OCA].  
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.M.]]
[[Category: Berman, H M.]]
[[Category: Camacho, N.P.]]
[[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.R.]]
[[Category: Smith, D R.]]
[[Category: Young, P.R.]]
[[Category: Young, P R.]]
[[Category: cytokine]]
[[Category: cytokine]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:18:25 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:32 2008''