CHEMISTRY OF ANTIBODY-BINDING TO A PROTEIN
CHEMISTRY OF ANTIBODY-BINDING TO A PROTEIN
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DOI：
10.1126/science.3823878
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发表时间：
1987-03-06
期刊：
影响因子：
56.9
通讯作者：
LERNER, RA
中科院分区：
文献类型：
--
作者：
GEYSEN, HM;TAINER, JA;LERNER, RA
通过对肌赤氰菊酯蛋白的抗原性与该蛋白序列的肽同源物进行比对，研究了抗体识别的化学性质。结果表明，整个蛋白表面具有抗原性，但存在针对特定位点的抗体的可能性受到局部立体化学的影响。虽然抗体结合域可以接近，但反应性最低的位置聚集在最紧密和最不移动的区域，并且与分子表面含有结合水分子的狭窄凹槽密切相关。最常被识别的位置形成三维超组装体，其特点是高局部迁移率，凸表面形状，通常具有负静电势。
The chemistry of antibody recognition was studied by mapping the antigenicity of the protein myohemerythrin with peptide homologs of the protein sequence. The results suggest that the entire protein surface is antigenic, but the probability of there being antibodies to a given site is influenced by local stereochemistry. Although accessible to an antibody binding domain, the least reactive positions cluster in the most tightly packed and least mobile regions and are closely associated with narrow, concave grooves in the molecular surface containing bound water molecules. The most frequently recognized sites form three-dimensional superassemblies characterized by high local mobility, convex surface shape, and often by negative electrostatic potential.