2FRG

Structure of the immunoglobulin-like domain of human TLT-1

2FRG の概要

• エントリーDOI: 10.2210/pdb2frg/pdb
• 分子名称: trem-like transcript-1 (2 entities in total)
• 機能のキーワード: immunoglobulin-like, beta-sandwich, cell surface receptor, triggering receptor, trem-like, platelet receptor, itim, immune system
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane ; Single-pass type I membrane protein : Q86YW5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11523.27

構造登録者

Gattis, J.L.,Lubkowski, J. (登録日: 2006-01-19, 公開日: 2006-03-14, 最終更新日: 2024-11-06)

主引用文献

Gattis, J.L.,Washington, A.V.,Chisholm, M.M.,Quigley, L.,Szyk, A.,McVicar, D.W.,Lubkowski, J.
The structure of the extracellular domain of triggering receptor expressed on myeloid cells like transcript-1 and evidence for a naturally occurring soluble fragment.
J.Biol.Chem., 281:13396-13403, 2006

PubMed Abstract: Triggering receptor expressed on myeloid cells like transcript-1 (TLT-1) is an abundant platelet-specific, type I transmembrane receptor. The extracellular fragment of TLT-1 consists of a single, immunoglobulin-like domain connected to the platelet cell membrane by a linker region called the stalk. Here we present evidence that a soluble fragment of the TLT-1 extracellular domain is found in serum of humans and mice and that an isoform of similar mass is released from platelets following activation with thrombin. We also report the crystal structure of the immunoglobulin domain of TLT-1 determined at the resolution of 1.19 A. The structure of TLT-1 is similar to other immunoglobulin-like variable domains, particularly those of triggering receptor expressed on myeloid cells-1 (TREM-1), the natural killer cell-activating receptor NKp44, and the polymeric immunoglobulin receptor. Particularly interesting is a 17-amino acid segment of TLT-1, homologous to a fragment of murine TREM-1, which, in turn, showed activity in blocking the TREM-1-mediated inflammatory responses in mice. Structural similarity to TREM-1 and polymeric immunoglobulin receptor, and evidence for a naturally occurring soluble fragment of the TLT-1 extracellular domain, suggest that this immunoglobulin-like domain autonomously plays an as yet unidentified, functional role.

PubMed: 16505478
DOI: 10.1074/jbc.M600489200

実験手法

X-RAY DIFFRACTION (1.19 Å)