1inr: Difference between revisions

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==Overview==

The crystal structure of recombinant human interleukin 10 (rhIL-10) has, been determined by X-ray crystallography at 2.0 A resolution. Interleukin, 10 is a dimer composed of identical polypeptide chains related by a 2-fold, axis. The molecule is predominantly alpha-helical. The main-chain fold, resembles that of interferon gamma (IFN-gamma) in which the structural, integrity of each domain is dependent on the intertwining of helices from, each peptide chain. Comparison of rhIL-10 and IFN-gamma reveals, differences in helix lengths and orientations of the 2-fold related, domains. Interleukin 10 and IFN-gamma contain several conserved residues, in their internal cores which suggest a possible "fingerprint" for, detection of other members of this fold.

The crystal structure of recombinant human interleukin 10 (rhIL-10) has been determined by X-ray crystallography at 2.0 A resolution. Interleukin 10 is a dimer composed of identical polypeptide chains related by a 2-fold axis. The molecule is predominantly alpha-helical. The main-chain fold resembles that of interferon gamma (IFN-gamma) in which the structural integrity of each domain is dependent on the intertwining of helices from each peptide chain. Comparison of rhIL-10 and IFN-gamma reveals differences in helix lengths and orientations of the 2-fold related domains. Interleukin 10 and IFN-gamma contain several conserved residues in their internal cores which suggest a possible "fingerprint" for detection of other members of this fold.

==Disease==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Walter, M.R.]]

[[Category: Walter, M R.]]

[[Category: cytokine]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:02:39 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:40 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The crystal structure of recombinant human interleukin 10 (rhIL-10) has, been determined by X-ray crystallography at 2.0 A resolution. Interleukin, 10 is a dimer composed of identical polypeptide chains related by a 2-fold, axis. The molecule is predominantly alpha-helical. The main-chain fold, resembles that of interferon gamma (IFN-gamma) in which the structural, integrity of each domain is dependent on the intertwining of helices from, each peptide chain. Comparison of rhIL-10 and IFN-gamma reveals, differences in helix lengths and orientations of the 2-fold related, domains. Interleukin 10 and IFN-gamma contain several conserved residues, in their internal cores which suggest a possible "fingerprint" for, detection of other members of this fold.
+The crystal structure of recombinant human interleukin 10 (rhIL-10) has been determined by X-ray crystallography at 2.0 A resolution. Interleukin 10 is a dimer composed of identical polypeptide chains related by a 2-fold axis. The molecule is predominantly alpha-helical. The main-chain fold resembles that of interferon gamma (IFN-gamma) in which the structural integrity of each domain is dependent on the intertwining of helices from each peptide chain. Comparison of rhIL-10 and IFN-gamma reveals differences in helix lengths and orientations of the 2-fold related domains. Interleukin 10 and IFN-gamma contain several conserved residues in their internal cores which suggest a possible "fingerprint" for detection of other members of this fold.
 ==Disease==
@@ Line 16: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Walter, M.R.]]
+[[Category: Walter, M R.]]
 [[Category: cytokine]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:02:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:40 2008''