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1B5L

OVINE INTERFERON TAU

1B5L の概要
エントリーDOI10.2210/pdb1b5l/pdb
分子名称INTERFERON TAU, SULFATE ION (3 entities in total)
機能のキーワードcytokine
由来する生物種Pichia pastoris
タンパク質・核酸の鎖数1
化学式量合計20127.81
構造登録者
Radhakrishnan, R.,Walter, L.J.,Subramaniam, P.S.,Johnson, H.J.,Walter, M.R. (登録日: 1999-01-07, 公開日: 1999-05-18, 最終更新日: 2024-10-30)
主引用文献Radhakrishnan, R.,Walter, L.J.,Subramaniam, P.S.,Johnson, H.M.,Walter, M.R.
Crystal structure of ovine interferon-tau at 2.1 A resolution.
J.Mol.Biol., 286:151-162, 1999
Cited by
PubMed Abstract: 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.
PubMed: 9931256
DOI: 10.1006/jmbi.1998.2480
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.1 Å)
構造検証レポート
Validation report summary of 1b5l
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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