3IP2

Crystal structure of red fluorescent protein Neptune at pH 7.0

3IP2 の概要

• エントリーDOI: 10.2210/pdb3ip2/pdb
• 分子名称: Neptune red fluorescent protein (2 entities in total)
• 機能のキーワード: fluorescent protein
• 由来する生物種: Entacmaea quadricolor
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27369.21

構造登録者

Lin, M.Z.,McKeown, M.R.,Ng, H.L.,Aguilera, T.A.,Shaner, N.C.,Ma, W.,Adams, S.R.,Campbell, R.E.,Alber, T.,Tsien, R.Y. (登録日: 2009-08-15, 公開日: 2009-12-15, 最終更新日: 2023-11-22)

主引用文献

Lin, M.Z.,McKeown, M.R.,Ng, H.L.,Aguilera, T.A.,Shaner, N.C.,Campbell, R.E.,Adams, S.R.,Gross, L.A.,Ma, W.,Alber, T.,Tsien, R.Y.
Autofluorescent proteins with excitation in the optical window for intravital imaging in mammals.
Chem.Biol., 16:1169-1179, 2009

PubMed Abstract: Fluorescent proteins have become valuable tools for biomedical research as protein tags, reporters of gene expression, biosensor components, and cell lineage tracers. However, applications of fluorescent proteins for deep tissue imaging in whole mammals have been constrained by the opacity of tissues to excitation light below 600 nm, because of absorbance by hemoglobin. Fluorescent proteins that excite efficiently in the "optical window" above 600 nm are therefore highly desirable. We report here the evolution of far-red fluorescent proteins with peak excitation at 600 nm or above. The brightest one of these, Neptune, performs well in imaging deep tissues in living mice. The crystal structure of Neptune reveals a novel mechanism for red-shifting involving the acquisition of a new hydrogen bond with the acylimine region of the chromophore.

PubMed: 19942140
DOI: 10.1016/j.chembiol.2009.10.009

実験手法

X-RAY DIFFRACTION (1.6 Å)