Standard conformations for the canonical structures of immunoglobulins
Standard conformations for the canonical structures of immunoglobulins
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DOI：
10.1006/jmbi.1997.1354
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发表时间：
1997-11-07
影响因子：
5.6
通讯作者：
Chothia, C
中科院分区：
文献类型：
--
作者：
AlLazikani, B;Lesk, AM;Chothia, C
描述了在高分辨率下准确确定的17个免疫球蛋白结构中的L1，L2，L3，H1和H2高变区的主链构象的比较分析。这总共涉及79个高变区。我们还分析了15个V-H结构域中的12个的H3区的一部分，根据关键位点的残基，79个高变区可以归属于18种不同的典型结构之一。我们发现，这些高变区中有71个具有非常接近于可以定义为每个典型结构的“标准”构象的构象。这些标准的构象进行了详细描述。其他八个高变区与标准构象有很小的偏差，在六种情况下，只涉及单个肽组的旋转。大多数H3高变区在靠近框架的部分具有相同的构象，并且这里也描述了这种构象的细节。(C)出版社：Academic Press Limited。
A comparative analysis of the main-chain conformation of the L1, L2, L3, H1 and H2 hypervariable regions in 17 immunoglobulin structures that have been accurately determined at high resolution is described. This involves 79 hypervariable regions in all. We also analysed a part of the H3 region in 12 of the 15 V-H domains considered here.On the basis of the residues at key sites the 79 hypervariable regions can be assigned to one of 18 different canonical structures. We show that 71 of these hypervariable regions have a conformation that is very close to what can be defined as a ''standard'' conformation of each canonical structure. These standard conformations are described in detail. The other eight hypervariable regions have small deviations from the standard conformations that, in six cases, involve only the rotation of a single peptide group. Most H3 hypervariable regions have the same conformation in the part that is close to the framework and the details of this conformation are also described here. (C) 1997 Academic Press Limited.