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1hib
From Proteopedia
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| - | [[Image:1hib.gif|left|200px]] | + | [[Image:1hib.gif|left|200px]] |
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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''' | + | {{Structure |
| + | |PDB= 1hib |SIZE=350|CAPTION= <scene name='initialview01'>1hib</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HIB is a [ | + | 1HIB 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=1HIB OCA]. |
==Reference== | ==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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/8364024 8364024] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cytokine]] | [[Category: cytokine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:37:24 2008'' |
Revision as of 09:37, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 11:37:24 2008
