1rcb: Difference between revisions

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==Overview==
==Overview==
The crystal structure of human recombinant interleukin-4 (IL-4) has been, solved by multiple isomorphous replacement, and refined to an R factor of, 0.218 at 2.25 A resolution. The molecule is a left-handed four-helix, bundle with a short stretch of beta sheet. The structure bears close, resemblance to other cytokines such as granulocyte-macrophage colony, stimulating factor (GM-CSF). Although no sequence similarity of IL-4 to, GM-CSF and other related cytokines has been previously postulated, structure-based alignment of IL-4 and GM-CSF revealed that the core of the, molecules, including large parts of all four helices and extending over, half of the molecule, has 30% sequence identity. This may have identified, regions which are not only important to maintain structure, but could also, play a role in receptor binding.
The crystal structure of human recombinant interleukin-4 (IL-4) has been solved by multiple isomorphous replacement, and refined to an R factor of 0.218 at 2.25 A resolution. The molecule is a left-handed four-helix bundle with a short stretch of beta sheet. The structure bears close resemblance to other cytokines such as granulocyte-macrophage colony stimulating factor (GM-CSF). Although no sequence similarity of IL-4 to GM-CSF and other related cytokines has been previously postulated, structure-based alignment of IL-4 and GM-CSF revealed that the core of the molecules, including large parts of all four helices and extending over half of the molecule, has 30% sequence identity. This may have identified regions which are not only important to maintain structure, but could also play a role in receptor binding.


==Disease==
==Disease==
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[[Category: cytokine]]
[[Category: cytokine]]


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Revision as of 15:49, 21 February 2008

File:1rcb.gif


1rcb, resolution 2.25Å

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CRYSTAL STRUCTURE OF HUMAN RECOMBINANT INTERLEUKIN-4 AT 2.25 ANGSTROMS RESOLUTION

OverviewOverview

The crystal structure of human recombinant interleukin-4 (IL-4) has been solved by multiple isomorphous replacement, and refined to an R factor of 0.218 at 2.25 A resolution. The molecule is a left-handed four-helix bundle with a short stretch of beta sheet. The structure bears close resemblance to other cytokines such as granulocyte-macrophage colony stimulating factor (GM-CSF). Although no sequence similarity of IL-4 to GM-CSF and other related cytokines has been previously postulated, structure-based alignment of IL-4 and GM-CSF revealed that the core of the molecules, including large parts of all four helices and extending over half of the molecule, has 30% sequence identity. This may have identified regions which are not only important to maintain structure, but could also play a role in receptor binding.

DiseaseDisease

Known diseases associated with this structure: AIDS, slow progression to OMIM:[147781], Atopy, susceptibility to OMIM:[147781]

About this StructureAbout this Structure

1RCB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of human recombinant interleukin-4 at 2.25 A resolution., Wlodawer A, Pavlovsky A, Gustchina A, FEBS Lett. 1992 Aug 31;309(1):59-64. PMID:1511746

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