5LF2

Crystal structure of laminin beta2 LE5-LF-LE6

5LF2 の概要

• エントリーDOI: 10.2210/pdb5lf2/pdb
• 分子名称: Laminin subunit beta-2, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: extracellular matrix, cell adhesion
• 由来する生物種: Rattus norvegicus (Norway Rat)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix, basement membrane: P15800
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69181.89

構造登録者

Pulido, D.,Hohenester, E. (登録日: 2016-06-30, 公開日: 2016-07-27, 最終更新日: 2024-10-09)

主引用文献

Pulido, D.,Briggs, D.C.,Hua, J.,Hohenester, E.
Crystallographic analysis of the laminin beta 2 short arm reveals how the LF domain is inserted into a regular array of LE domains.
Matrix Biol., 57-58:204-212, 2017

PubMed Abstract: Laminins are a major constituent of all basement membranes. The polymerisation of laminins at the cell surface is mediated by the three short arms of the cross-shaped laminin heterotrimer. The short arms contain repeats of laminin-type epidermal growth factor-like (LE) domains, interspersed with globular domains of unknown function. A single LF domain is inserted between LE5 and LE6 of the laminin β1 and β2 chains. We report the crystal structure at 1.85Å resolution of the laminin β2 LE5-LF-LE6 region. The LF domain consists of a β-sandwich related to bacterial family 35 carbohydrate binding modules, and more distantly to the L4 domains present in the short arms of laminin α and γ chains. An α-helical region mediates the extensive interaction of the LF domain with LE5. The relative arrangement of LE5 and LE6 is very similar to that of consecutive LE domains in uninterrupted LE tandems. Fitting atomic models to a low-resolution structure of the first eight domains of the laminin β1 chain determined by small-angle X-ray scattering suggests a deviation from the regular LE array at the LE4-LE5 junction. These results advance our understanding of laminin structure.

PubMed: 27425256
DOI: 10.1016/j.matbio.2016.06.006

実験手法

X-RAY DIFFRACTION (1.85 Å)