1b5l
From Proteopedia
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|PDB= 1b5l |SIZE=350|CAPTION= <scene name='initialview01'>1b5l</scene>, resolution 2.1Å | |PDB= 1b5l |SIZE=350|CAPTION= <scene name='initialview01'>1b5l</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5l OCA], [http://www.ebi.ac.uk/pdbsum/1b5l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b5l RCSB]</span> | ||
}} | }} | ||
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[[Category: Walter, L J.]] | [[Category: Walter, L J.]] | ||
[[Category: Walter, M R.]] | [[Category: Walter, M R.]] | ||
- | [[Category: SO4]] | ||
[[Category: cytokine]] | [[Category: cytokine]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:54:11 2008'' |
Revision as of 15:54, 30 March 2008
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, resolution 2.1Å | |||||||
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Ligands: | |||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
OVINE INTERFERON TAU
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.
About this Structure
1B5L is a Single protein structure of sequence from Pichia pastoris. Full crystallographic information is available from OCA.
Reference
Crystal structure of ovine interferon-tau at 2.1 A resolution., Radhakrishnan R, Walter LJ, Subramaniam PS, Johnson HM, Walter MR, J Mol Biol. 1999 Feb 12;286(1):151-62. PMID:9931256
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