1b5l: Difference between revisions

Line 1:

[[Image:1b5l.jpg|left|200px]]<br /><applet load="1b5l" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1b5l.jpg|left|200px]]<br /><applet load="1b5l" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1b5l, resolution 2.1Å" />

'''OVINE INTERFERON TAU'''<br />

==Overview==

Ovine interferon-tau (ovIFN-tau) is a pregnancy recognition hormone, required for normal embryonic development in sheep. In addition to its, novel role in reproductive physiology, ovIFN-tau displays antiviral and, antiproliferative activities similar to the IFN-alpha subtypes. To probe, the structural basis for its unique activity profile, the crystal, structure of ovIFN-tau has been determined at 2.1 A resolution. The fold, of ovIFN-tau is similar to the previously determined crystal structures of, human IFN-alpha2b and human and murine IFN-beta, which each contain five, alpha-helices. Comparison of ovIFN-tau with huIFN-alpha2b, huIFN-beta, and, muIFN-beta reveals unexpected structural differences that occur in regions, of considerable sequence identity. Specifically, main-chain differences up, to 11 A occur for residues in helix A, the AB loop, helix B, and the BC, loop. Furthermore, these regions are known to be important for receptor, binding and biological activity. Of particular interest, a buried ion pair, is observed in ovIFN-tau between Glu71 and Arg145 which displaces a, conserved tryptophan residue (Trp77) from the helical bundle core. This, ion pair represents a major change in the core of ovIFN-tau compared to, huIFN-alpha2b. Based on amino acid sequence comparisons, these ovIFN-tau, structural features may be conserved in several human IFN-alpha subtypes, and IFN-omega. The structure identifies potential problems in interpreting, site-directed mutagenesis data on the human IFN-alpha family that consists, of 12 proteins.

Ovine interferon-tau (ovIFN-tau) is a pregnancy recognition hormone required for normal embryonic development in sheep. In addition to its novel role in reproductive physiology, ovIFN-tau displays antiviral and antiproliferative activities similar to the IFN-alpha subtypes. To probe the structural basis for its unique activity profile, the crystal structure of ovIFN-tau has been determined at 2.1 A resolution. The fold of ovIFN-tau is similar to the previously determined crystal structures of human IFN-alpha2b and human and murine IFN-beta, which each contain five alpha-helices. Comparison of ovIFN-tau with huIFN-alpha2b, huIFN-beta, and muIFN-beta reveals unexpected structural differences that occur in regions of considerable sequence identity. Specifically, main-chain differences up to 11 A occur for residues in helix A, the AB loop, helix B, and the BC loop. Furthermore, these regions are known to be important for receptor binding and biological activity. Of particular interest, a buried ion pair is observed in ovIFN-tau between Glu71 and Arg145 which displaces a conserved tryptophan residue (Trp77) from the helical bundle core. This ion pair represents a major change in the core of ovIFN-tau compared to huIFN-alpha2b. Based on amino acid sequence comparisons, these ovIFN-tau structural features may be conserved in several human IFN-alpha subtypes and IFN-omega. The structure identifies potential problems in interpreting site-directed mutagenesis data on the human IFN-alpha family that consists of 12 proteins.

==About this Structure==

1B5L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_pastoris Pichia pastoris] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1B5L OCA].

1B5L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_pastoris Pichia pastoris] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5L OCA].

==Reference==

Line 13:

[[Category: Pichia pastoris]]

[[Category: Single protein]]

[[Category: Johnson, H.J.]]

[[Category: Johnson, H J.]]

[[Category: Radhakrishnan, R.]]

[[Category: Subramaniam, P.S.]]

[[Category: Subramaniam, P S.]]

[[Category: Walter, L.J.]]

[[Category: Walter, L J.]]

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

[[Category: Walter, M R.]]

[[Category: SO4]]

[[Category: cytokine]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 11:22:~~54 2007~~''

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@@ Line 1: / Line 1: @@
-[[Image:1b5l.jpg|left|200px]]<br /><applet load="1b5l" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1b5l.jpg|left|200px]]<br /><applet load="1b5l" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1b5l, resolution 2.1&Aring;" />
 '''OVINE INTERFERON TAU'''<br />
 ==Overview==
-Ovine interferon-tau (ovIFN-tau) is a pregnancy recognition hormone, required for normal embryonic development in sheep. In addition to its, novel role in reproductive physiology, ovIFN-tau displays antiviral and, antiproliferative activities similar to the IFN-alpha subtypes. To probe, the structural basis for its unique activity profile, the crystal, structure of ovIFN-tau has been determined at 2.1 A resolution. The fold, of ovIFN-tau is similar to the previously determined crystal structures of, human IFN-alpha2b and human and murine IFN-beta, which each contain five, alpha-helices. Comparison of ovIFN-tau with huIFN-alpha2b, huIFN-beta, and, muIFN-beta reveals unexpected structural differences that occur in regions, of considerable sequence identity. Specifically, main-chain differences up, to 11 A occur for residues in helix A, the AB loop, helix B, and the BC, loop. Furthermore, these regions are known to be important for receptor, binding and biological activity. Of particular interest, a buried ion pair, is observed in ovIFN-tau between Glu71 and Arg145 which displaces a, conserved tryptophan residue (Trp77) from the helical bundle core. This, ion pair represents a major change in the core of ovIFN-tau compared to, huIFN-alpha2b. Based on amino acid sequence comparisons, these ovIFN-tau, structural features may be conserved in several human IFN-alpha subtypes, and IFN-omega. The structure identifies potential problems in interpreting, site-directed mutagenesis data on the human IFN-alpha family that consists, of 12 proteins.
+Ovine interferon-tau (ovIFN-tau) is a pregnancy recognition hormone required for normal embryonic development in sheep. In addition to its novel role in reproductive physiology, ovIFN-tau displays antiviral and antiproliferative activities similar to the IFN-alpha subtypes. To probe the structural basis for its unique activity profile, the crystal structure of ovIFN-tau has been determined at 2.1 A resolution. The fold of ovIFN-tau is similar to the previously determined crystal structures of human IFN-alpha2b and human and murine IFN-beta, which each contain five alpha-helices. Comparison of ovIFN-tau with huIFN-alpha2b, huIFN-beta, and muIFN-beta reveals unexpected structural differences that occur in regions of considerable sequence identity. Specifically, main-chain differences up to 11 A occur for residues in helix A, the AB loop, helix B, and the BC loop. Furthermore, these regions are known to be important for receptor binding and biological activity. Of particular interest, a buried ion pair is observed in ovIFN-tau between Glu71 and Arg145 which displaces a conserved tryptophan residue (Trp77) from the helical bundle core. This ion pair represents a major change in the core of ovIFN-tau compared to huIFN-alpha2b. Based on amino acid sequence comparisons, these ovIFN-tau structural features may be conserved in several human IFN-alpha subtypes and IFN-omega. The structure identifies potential problems in interpreting site-directed mutagenesis data on the human IFN-alpha family that consists of 12 proteins.
 ==About this Structure==
-B5L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_pastoris Pichia pastoris] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B5L OCA].
+B5L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_pastoris Pichia pastoris] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5L OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Pichia pastoris]]
 [[Category: Single protein]]
-[[Category: Johnson, H.J.]]
+[[Category: Johnson, H J.]]
 [[Category: Radhakrishnan, R.]]
-[[Category: Subramaniam, P.S.]]
+[[Category: Subramaniam, P S.]]
-[[Category: Walter, L.J.]]
+[[Category: Walter, L J.]]
-[[Category: Walter, M.R.]]
+[[Category: Walter, M R.]]
 [[Category: SO4]]
 [[Category: cytokine]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:22:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:45 2008''