1OKI

Crystal structure of truncated human beta-B1-crystallin

1OKI の概要

• エントリーDOI: 10.2210/pdb1oki/pdb
• 分子名称: BETA CRYSTALLIN B1 (2 entities in total)
• 機能のキーワード: crystallin, cataract, eye lens protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48504.18

構造登録者

van Montfort, R.L.M.,Bateman, O.A.,Lubsen, N.H.,Slingsby, C. (登録日: 2003-07-25, 公開日: 2004-01-22, 最終更新日: 2024-11-06)

主引用文献

Van Montfort, R.L.M.,Bateman, O.A.,Lubsen, N.H.,Slingsby, C.
Crystal Structure of Truncated Human Beta-B1-Crystallin
Protein Sci., 12:2606-, 2003

PubMed Abstract: Crystallins are long-lived proteins packed inside eye lens fiber cells that are essential in maintaining the transparency and refractive power of the eye lens. Members of the two-domain betagamma-crystallin family assemble into an array of oligomer sizes, forming intricate higher-order networks in the lens cell. Here we describe the 1.4 angstroms resolution crystal structure of a truncated version of human betaB1 that resembles an in vivo age-related truncation. The structure shows that unlike its close homolog, betaB2-crystallin, the homodimer is not domain swapped, but its domains are paired intramolecularly, as in more distantly related monomeric gamma-crystallins. However, the four-domain dimer resembles one half of the crystallographic bovine betaB2 tetramer and is similar to the engineered circular permuted rat betaB2. The crystal structure shows that the truncated betaB1 dimer is extremely well suited to form higher-order lattice interactions using its hydrophobic surface patches, linker regions, and sequence extensions.

PubMed: 14573871
DOI: 10.1110/PS.03265903

実験手法

X-RAY DIFFRACTION (1.4 Å)