Structure and function of LIM domains.
Structure and function of LIM domains.
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DOI：
10.1007/978-3-642-80481-6_4
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发表时间：
1998
影响因子：
--
通讯作者：
L. Jurata;G. Gill
中科院分区：
文献类型：
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作者：
L. Jurata;G. Gill
在许多蛋白质中发现的保守结构域提供了与其他蛋白质相互作用的表面。这样的结构域折叠独立于蛋白质的其余部分，并且在一类结构域内结构相似。一类的个体成员具有足够的序列变异以提供对特定靶序列的高特异性。因此，在进化中，保守的结构被保留，但变异被选择提供特定的功能。分子识别是生物学中的基本性质，长期以来在免疫学（抗体、T和B细胞受体）和内分泌学（激素受体）中被认识到，并且最近在细胞内信号转导和转录过程中被认识到。蛋白质通常含有一个以上的相同或不同类别的结构域，这些结构域提供分子复合物的组装。本专著中讨论的结构域通常为40-100个氨基酸，识别靶蛋白中相对较短但特异的序列。在组合中，域和
Conserved domains found in many proteins provide surfaces that interact with other proteins. Such domains fold independently of the remainder of the protein and are structurally similar within a class of domains. Individual members of a class have sufficient sequence variation to provide high specificity for particular target sequences. Thus, in evolution, conserved structures were retained but variations were selected that provided specific function. Molecular recognition is a fundamental property in biology, long recognized in immunology (antibodies, T and B cell receptors) and in endocrinology (hormone receptors) and more recently appreciated in intracellular signal transduction and transcription processes. Proteins often contain more than one domain either of the same or of a different class that provide for assembly of molecular complexes. The domains discussed in this monograph are in general 40-100 amino acids in length and recognize relatively short but specific sequences in target proteins. In combination, domains and