2BWL

Murine angiogenin, phosphate complex

2BWL の概要

• エントリーDOI: 10.2210/pdb2bwl/pdb
• 関連するPDBエントリー: 2BWK
• 分子名称: ANGIOGENIN, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: ribonuclease, angiogenesis, cancer, hydrolase
• 由来する生物種: MUS MUSCULUS (MOUSE)
• 細胞内の位置: Secreted: P21570
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13982.60

構造登録者

Holloway, D.E.,Chavali, G.B.,Hares, M.C.,Subramanian, V.,Acharya, K.R. (登録日: 2005-07-15, 公開日: 2005-11-30, 最終更新日: 2024-11-13)

主引用文献

Holloway, D.E.,Chavali, G.B.,Hares, M.C.,Subramanian, V.,Acharya, K.R.
Structure of Murine Angiogenin: Features of the Substrate- and Cell-Binding Regions and Prospects for Inhibitor-Binding Studies.
Acta Crystallogr.,Sect.D, 61:1568-, 2005

PubMed Abstract: Angiogenin is an unusual member of the pancreatic ribonuclease superfamily that induces blood-vessel formation and is a promising anticancer target. The three-dimensional structure of murine angiogenin (mAng) has been determined by X-ray crystallography. Two structures are presented: one is a complex with sulfate ions (1.5 Angstroms resolution) and the other a complex with phosphate ions (1.6 Angstroms resolution). Residues forming the putative B(1), P(1) and B(2) subsites occupy positions similar to their hAng counterparts and are likely to play similar roles. The anions occupy the P(1) subsite, sulfate binding conventionally and phosphate adopting two orientations, one of which is novel. The B(1) subsite is obstructed by Glu116 and Phe119, with the latter assuming a less invasive position than its hAng counterpart. Hydrophobic interactions between the C-terminal segment and the main body of the protein are more extensive than in hAng and may underly the lower enzymatic activity of the murine protein. Elsewhere, the structure of the H3-B2 loop supports the view that hAng Asn61 interacts directly with cell-surface molecules and does not merely stabilize adjacent regions of the hAng structure. mAng crystals appear to offer small-molecule inhibitors a clear route to the active site and may even withstand a reorientation of the C-terminal segment that provides access to the cryptic B(1) subsite. These features represent considerable advantages over crystalline hAng and bAng.

PubMed: 16301790
DOI: 10.1107/S0907444905029616

実験手法

X-RAY DIFFRACTION (1.62 Å)