Zhang Jianhua, Chen Yong, Gao Feng, Chen Weihong, Qi Jianxun, Xia Chun
Department of Microbiology and Immunology, College of Veterinary Medicine, China Agricultural University, Beijing 100094, People's Republic of China.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):99-101. doi: 10.1107/S174430910905088X. Epub 2009 Dec 25.
In order to understand the biological properties of the immune systems of waterfowl and to establish a system for structural studies of duck class I major histocompatibility complex (DuMHC I), a complex of DuMHC I with duck beta(2)-microglobulin (Dubeta(2)m) and the peptide AEIEDLIF (AF8) derived from H5N1 NP residues 251-258 was assembled. The complex was crystallized; the crystals belonged to space group C222(1), with unit-cell parameters a = 54.7, b = 72.4, c = 102.2 A, and diffracted to 2.3 A resolution. Matthews coefficient calculation and initial structure determination by molecular replacement showed that the crystals did not contain the whole DuMHC I complex, but instead contained the DuMHC I alpha3 domain and a Dubeta2m molecule (DuMHC I alpha3+beta2m). Another complex of DuMHC I with the peptide IDWFDGKE derived from a chicken fusion protein also generated the same results. The stable structure of DuMHC I alpha3+beta2m may reflect some unique characteristics of DuMHC I and pave the way for novel MHC structure-related studies in the future.
为了解水禽免疫系统的生物学特性并建立鸭 I 类主要组织相容性复合体（DuMHC I）的结构研究体系，组装了 DuMHC I 与鸭β2-微球蛋白（Dubeta2m）以及源自 H5N1 NP 残基 251 - 258 的肽 AEIEDLIF（AF8）的复合物。该复合物被结晶；晶体属于空间群 C222(1)，晶胞参数 a = 54.7、b = 72.4、c = 102.2 Å，并衍射到 2.3 Å 分辨率。马修斯系数计算和通过分子置换进行的初始结构测定表明，晶体并不包含完整的 DuMHC I 复合物，而是包含 DuMHC I α3 结构域和一个 Dubeta2m 分子（DuMHC I α3 + β2m）。DuMHC I 与源自鸡融合蛋白的肽 IDWFDGKE 的另一个复合物也产生了相同的结果。DuMHC I α3 + β2m 的稳定结构可能反映了 DuMHC I 的一些独特特性，并为未来新的 MHC 结构相关研究铺平了道路。
