Ninjurin1细胞外N端结构域的1H、13C和15N化学位移归属

1H, 13C and 15N chemical shift assignments of Ninjurin1 Extracellular N-terminal Domain.

作者信息

Lee In-Gyun, Jang Sun-Bok, Kim Ji-Hun, Lee Ki-Young, Lee Kyu-Yeon, Cheong Hae-Kap, Lee Bong-Jin

机构信息

The Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, San 56-1, Shillim-Dong, Kwanak-Gu, Seoul 151-742, Korea.

出版信息

Biomol NMR Assign. 2013 Oct;7(2):159-62. doi: 10.1007/s12104-012-9400-3. Epub 2012 Jun 15.

DOI:10.1007/s12104-012-9400-3

Abstract

Cell adhesion molecules play a crucial role in fundamental biological processes via regulating cell-cell interactions. Nerve injury induced protein1 (Ninjurin1) is a novel adhesion protein that has no significant homology with other known cell adhesion molecules. Here we present the assignment of an 81 aa construct for human Ninjurin1 Extracellular N-Terminal (ENT) domain, which comprises the critical adhesion domain.

摘要

细胞粘附分子通过调节细胞间相互作用在基本生物学过程中发挥关键作用。神经损伤诱导蛋白1（Ninjurin1）是一种新型粘附蛋白，与其他已知细胞粘附分子没有明显的同源性。在此，我们展示了人Ninjurin1细胞外N端（ENT）结构域（包含关键粘附结构域）的一个81个氨基酸构建体的分配情况。

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