1rcb: Difference between revisions

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==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==

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[[Category: cytokine]]

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@@ Line 4: / Line 4: @@
 ==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==
@@ Line 21: / Line 21: @@
 [[Category: cytokine]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:48:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:19 2008''