1Z2F
solution structure of CfAFP-501
1Z2F の概要
| エントリーDOI | 10.2210/pdb1z2f/pdb |
| NMR情報 | BMRB: 6111 |
| 分子名称 | Antifreeze Protein Isoform 501 (1 entity in total) |
| 機能のキーワード | antifreeze protein, choristoneura fumiferana, spruce budworm, solution structure |
| 由来する生物種 | Choristoneura fumiferana (spruce budworm) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12546.90 |
| 構造登録者 | |
| 主引用文献 | Li, C.,Guo, X.,Jia, Z.,Xia, B.,Jin, C. Solution Structure of an Antifreeze Protein CfAFP-501 from Choristoneura fumiferana J.Biomol.Nmr, 32:251-256, 2005 Cited by PubMed Abstract: Antifreeze proteins (AFPs) are widely employed by various organisms as part of their overwintering survival strategy. AFPs have the unique ability to suppress the freezing point of aqueous solution and inhibit ice recrystallization through binding to the ice seed crystals and restricting their growth. The solution structure of CfAFP-501 from spruce budworm has been determined by NMR spectroscopy. Our result demonstrates that CfAFP-501 retains its rigid and highly regular structure in solution. Overall, the solution structure is similar to the crystal structure except the N- and C-terminal regions. NMR spin-relaxation experiments further indicate the overall rigidity of the protein and identify a collection of residues with greater flexibilities. Furthermore, Pro91 shows a cis conformation in solution instead of the trans conformation determined in the crystal structure. PubMed: 16132825DOI: 10.1007/s10858-005-8206-3 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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