1P53

The Crystal Structure of ICAM-1 D3-D5 fragment

1P53 の概要

• エントリーDOI: 10.2210/pdb1p53/pdb
• 分子名称: Intercellular adhesion molecule-1, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: igsf domain, beta-sheet, dimer, cell adhesion
• 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: 58986.23

構造登録者

Yang, Y.,Jun, C.D.,Liu, J.H.,Zhang, R.,Jochimiak, A.,Springer, T.A.,Wang, J.H. (登録日: 2003-04-24, 公開日: 2004-05-04, 最終更新日: 2024-10-09)

主引用文献

Yang, Y.,Jun, C.D.,Liu, J.H.,Zhang, R.,Joachimiak, A.,Springer, T.A.,Wang, J.H.
Structural basis for dimerization of ICAM-1 on the cell surface.
Mol.Cell, 14:269-276, 2004

PubMed Abstract: We have determined the 3.0 A crystal structure of the three C-terminal domains 3-5 (D3-D5) of ICAM-1. Combined with the previously known N-terminal two-domain structure (D1D2), a model of an entire ICAM-1 extracellular fragment has been constructed. This model should represent a general architecture of other ICAM family members, particularly ICAM-3 and ICAM-5. The observed intimate dimerization interaction at D4 and a stiff D4-D5 stem-like architecture provide a good structural explanation for the existence of preformed ICAM-1 cis dimers on the cell membrane. Together with another dimerization interface at D1, a band-like one-dimensional linear cluster of ICAM-1 on an antigen-presenting cell (APC) surface can be envisioned, which might explain the formation of an immunological synapse between an activated T cell and APC which is critical for T cell receptor signaling.

PubMed: 15099525
DOI: 10.1016/S1097-2765(04)00204-7

実験手法

X-RAY DIFFRACTION (3.06 Å)