II类组织相容性蛋白HLA-DR1的结构同源性模型的准确性：与晶体结构的比较

Accuracy of a structural homology model for a class II histocompatibility protein, HLA-DR1: comparison to the crystal structure.

作者信息

Nauss J L, Reid R H, Sadegh-Nasseri S

机构信息

Department of Gastroenterology, Walter Reed Army Institute of Research, Washington, D.C. 20307-5100, USA.

出版信息

J Biomol Struct Dyn. 1995 Jun;12(6):1213-33. doi: 10.1080/07391102.1995.10508808.

DOI:10.1080/07391102.1995.10508808

PMID:7669268

Abstract

Structural homology modeling is used to test the accuracy by which a Class I major histocompatibility complex (MHC) could be used to model a Class II MHC. The crystal structure of HLA-aw68 served as a reference molecule to model HLA-DR1. The resulting model was compared to the recently released crystal structure by Brown et al. (Nature, Vol. 364, p. 33-39 (1993)). The overall tertiary structure motif (two alpha-helices and a beta-sheet forming a peptide binding cleft) was maintained. However, significant deviations in the secondary structure elements were found between the model and the DR1 crystal structure. These deviations were consistent with the differences between Class I and Class II crystal structures. In regions where the model and DR1 crystals structures are most similar, side chain orientations are also similar. Specific peptide-MHC interactions are discussed and compared with the crystal structure results.

摘要

结构同源性建模用于测试将I类主要组织相容性复合体（MHC）用于模拟II类MHC的准确性。HLA-aw68的晶体结构用作模拟HLA-DR1的参考分子。将所得模型与Brown等人最近发表的晶体结构（《自然》，第364卷，第33 - 39页（1993年））进行比较。整体三级结构基序（由两条α螺旋和一条β折叠形成一个肽结合裂隙）得以保留。然而，在模型与DR1晶体结构之间发现了二级结构元件的显著偏差。这些偏差与I类和II类晶体结构之间的差异一致。在模型与DR1晶体结构最相似的区域，侧链取向也相似。文中讨论了特定的肽 - MHC相互作用，并与晶体结构结果进行了比较。