This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2int
From Proteopedia
(New page: 200px<br /> <applet load="2int" size="450" color="white" frame="true" align="right" spinBox="true" caption="2int, resolution 2.35Å" /> '''CRYSTAL STRUCTURE O...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2int.gif|left|200px]]<br /> | + | [[Image:2int.gif|left|200px]]<br /><applet load="2int" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2int" size=" | + | |
caption="2int, resolution 2.35Å" /> | caption="2int, resolution 2.35Å" /> | ||
'''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4'''<br /> | '''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of recombinant human interleukin-4 (rhuIL-4) was | + | The crystal structure of recombinant human interleukin-4 (rhuIL-4) was initially determined at 3.5-A resolution by multiple isomorphous replacement techniques and subsequently refined to a resolution of 2.35 A by simulated annealing. The final crystallographic R-factor, based on all data in the range 6.0-2.35 A (7470 reflections), is 0.232. Bond lengths and bond angles in the molecule have root mean square deviations from ideal values of 0.016 A and 2.4 degrees, respectively. The overall structure is highly compact and globular with a predominantly hydrophobic core. The main structural feature of rhuIL-4 is a four alpha-helix bundle, which composes approximately 58% of the structure. The helices are arranged in a left-handed antiparallel bundle with two overhand connections. Within these connections is a two-stranded antiparallel beta-sheet. Both the tertiary and secondary structures of rhuIL-4 are similar to those of human granulocyte-macrophage colony-stimulating factor. Critical regions for receptor binding are proposed. |
==Disease== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2INT 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:// | + | 2INT 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=2INT OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 16: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bugg, C | + | [[Category: Bugg, C E.]] |
| - | [[Category: Cook, W | + | [[Category: Cook, W J.]] |
| - | [[Category: Ealick, S | + | [[Category: Ealick, S E.]] |
| - | [[Category: Junior, R | + | [[Category: Junior, R Cameron.]] |
| - | [[Category: Junior, R | + | [[Category: Junior, R L.Walter.]] |
| - | [[Category: Nagabhushan, T | + | [[Category: Nagabhushan, T L.]] |
[[Category: Reichert, P.]] | [[Category: Reichert, P.]] | ||
| - | [[Category: Trotta, P | + | [[Category: Trotta, P P.]] |
| - | [[Category: Walter, M | + | [[Category: Walter, M R.]] |
| - | [[Category: Zhao, B | + | [[Category: Zhao, B G.]] |
[[Category: cytokine]] | [[Category: cytokine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:54:21 2008'' |
Revision as of 15:54, 21 February 2008
|
CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4
Contents |
Overview
The crystal structure of recombinant human interleukin-4 (rhuIL-4) was initially determined at 3.5-A resolution by multiple isomorphous replacement techniques and subsequently refined to a resolution of 2.35 A by simulated annealing. The final crystallographic R-factor, based on all data in the range 6.0-2.35 A (7470 reflections), is 0.232. Bond lengths and bond angles in the molecule have root mean square deviations from ideal values of 0.016 A and 2.4 degrees, respectively. The overall structure is highly compact and globular with a predominantly hydrophobic core. The main structural feature of rhuIL-4 is a four alpha-helix bundle, which composes approximately 58% of the structure. The helices are arranged in a left-handed antiparallel bundle with two overhand connections. Within these connections is a two-stranded antiparallel beta-sheet. Both the tertiary and secondary structures of rhuIL-4 are similar to those of human granulocyte-macrophage colony-stimulating factor. Critical regions for receptor binding are proposed.
Disease
Known diseases associated with this structure: AIDS, slow progression to OMIM:[147781], Atopy, susceptibility to OMIM:[147781]
About this Structure
2INT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of recombinant human interleukin-4., Walter MR, Cook WJ, Zhao BG, Cameron RP Jr, Ealick SE, Walter RL Jr, Reichert P, Nagabhushan TL, Trotta PP, Bugg CE, J Biol Chem. 1992 Oct 5;267(28):20371-6. PMID:1400355
Page seeded by OCA on Thu Feb 21 17:54:21 2008
