2int

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(New page: 200px<br /> <applet load="2int" size="450" color="white" frame="true" align="right" spinBox="true" caption="2int, resolution 2.35&Aring;" /> '''CRYSTAL STRUCTURE O...)
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<applet load="2int" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2int, resolution 2.35&Aring;" />
caption="2int, resolution 2.35&Aring;" />
'''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4'''<br />
'''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-4'''<br />
==Overview==
==Overview==
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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.
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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==
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==About this Structure==
==About this Structure==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2INT OCA].
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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==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bugg, C.E.]]
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[[Category: Bugg, C E.]]
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[[Category: Cook, W.J.]]
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[[Category: Cook, W J.]]
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[[Category: Ealick, S.E.]]
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[[Category: Ealick, S E.]]
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[[Category: Junior, R.Cameron.]]
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[[Category: Junior, R Cameron.]]
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[[Category: Junior, R.L.Walter.]]
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[[Category: Junior, R L.Walter.]]
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[[Category: Nagabhushan, T.L.]]
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[[Category: Nagabhushan, T L.]]
[[Category: Reichert, P.]]
[[Category: Reichert, P.]]
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[[Category: Trotta, P.P.]]
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[[Category: Trotta, P P.]]
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[[Category: Walter, M.R.]]
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[[Category: Walter, M R.]]
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[[Category: Zhao, B.G.]]
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[[Category: Zhao, B G.]]
[[Category: cytokine]]
[[Category: cytokine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:46:13 2007''
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''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


2int, resolution 2.35Å

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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

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