Callebaut I, Gilgès D, Vigon I, Mornon J P
Systèmes Moléculaires & Biologie Structurale, LMCP, CNRS UMR 7590, Université Paris 6, France.
Protein Sci. 2000 Jul;9(7):1382-90. doi: 10.1110/ps.9.7.1382.
Domains belonging to the immunoglobulin-like fold are responsible for a wide variety of molecular recognition processes. Here we describe a new family of domains, the HYR family, which is predicted to belong to this fold, and which appears to be involved in cellular adhesion. HYR domains were identified in several eukaryotic proteins, often associated with Complement Control Protein (CCP) modules or arranged in multiple copies. Our analysis provides a sequence and structural basis for understanding the role of these domains in interaction mechanisms and leads to further characterization of heretofore undescribed repeated domains with similar folds found in several bacterial proteins involved in enzymatic activities (some chitinases) or in cell surface adhesion (streptococcal C-alpha antigen).
属于免疫球蛋白样折叠的结构域负责多种分子识别过程。在此，我们描述了一个新的结构域家族，即HYR家族，预计它属于这种折叠结构，并且似乎参与细胞黏附。在几种真核生物蛋白质中鉴定出了HYR结构域，它们通常与补体控制蛋白（CCP）模块相关联或呈多个拷贝排列。我们的分析为理解这些结构域在相互作用机制中的作用提供了序列和结构基础，并促使对迄今未描述的具有相似折叠的重复结构域进行进一步表征，这些结构域存在于参与酶活性（一些几丁质酶）或细胞表面黏附（链球菌C-α抗原）的几种细菌蛋白质中。
