人骨髓瘤免疫球蛋白Fab'片段在2.0埃分辨率下的三维结构。
The three-dimensional structure of the fab' fragment of a human myeloma immunoglobulin at 2.0-angstrom resolution.
作者信息
Poljak R J, Amzel L M, Chen B L, Phizackerley R P, Saul F
出版信息
Proc Natl Acad Sci U S A. 1974 Sep;71(9):3440-4. doi: 10.1073/pnas.71.9.3440.
Abstract
The structural analysis of the Fab' fragment of human myeloma immunoglobulin IgGl(lambda) New has been extended to a nominal resolution of 2.0 A. Each of the structural subunits corresponding to the variable and to the constant homology regions of the light and heavy chains contains two irregular beta-sheets which are roughly parallel to each other and surround a tightly packed interior of hydrophobic side chains. About 50-60% of the amino-acid residues are included in beta-pleated sheets. Sequence alignments between the homology regions of Fab' New obtained by comparison of their three-dimensional structures are given. Some of the sequence variations observed in light and heavy chains and the role of the regions of hypervariable sequence in defining the size and shape of the active site of different immunoglobulin molecules are discussed on the basis of the three-dimensional model of Fab' New.
摘要
人骨髓瘤免疫球蛋白IgG1（λ）New的Fab'片段的结构分析已扩展至标称分辨率2.0埃。对应于轻链和重链可变区及恒定同源区的每个结构亚基均包含两个大致相互平行的不规则β折叠片层，它们围绕着由疏水侧链紧密堆积而成的内部区域。约50 - 60%的氨基酸残基包含在β折叠片中。给出了通过比较Fab' New的三维结构获得的同源区之间的序列比对。基于Fab' New的三维模型，讨论了在轻链和重链中观察到的一些序列变异以及高变序列区域在确定不同免疫球蛋白分子活性位点大小和形状方面的作用。
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The three-dimensional structure of the fab' fragment of a human myeloma immunoglobulin at 2.0-angstrom resolution.人骨髓瘤免疫球蛋白Fab'片段在2.0埃分辨率下的三维结构。
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