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首页> 外文期刊>Biochemistry >A MUTATIONAL ANALYSIS OF THE BINDING OF TWO DIFFERENT PROTEINS TO THE SAME ANTIBODY
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A MUTATIONAL ANALYSIS OF THE BINDING OF TWO DIFFERENT PROTEINS TO THE SAME ANTIBODY

机译：两种不同蛋白质与同一抗体结合的突变分析

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摘要

The crystal structures of the complexes between the anti-hen egg white lysozyme (HEL) antibody D1.3 and HEL and between D1.3 and the anti-D1.3 antibody E5.2 have shown that D1.3 contacts these two proteins through essentially the same set of combining site residues [Fields, B. A., Goldbaum, F. A., Ysern, X., Poljak, R. J., & Mariuzza, R. A. (1995) Nature 374, 739-742], To probe the relative contribution of individual residues to complex stabilization, single alanine substitutions were introduced in the combining site of D1.3, and their effects on affinity for HEL and for E5.2 were measured using surface plasmon resonance detection, fluorescence quench titration, or sedimentation equilibrium, The energetics of the binding to HEL are dominated by only 3 of the 13 contact residues tested (Delta G(mutant) - Delta G(wild type) > 2.5 kcal/mol): V(L)W92, V(H)D1C0, and V(H)Y101. These form a patch at the center of the interface and are surrounded by residues whose apparent contributions are much less pronounced (< 1.5 kcal/mol). This contrasts with the interaction of D1.3 with E5.2 in which most the contact residues (11 of 15) were found to play a significant role in ligand binding (> 1.5 kcal/mol). Furthermore, even though D1.3 contacts HEL and E5.2 in very similar ways, the functionally important residues of D1.3 are different for the two interactions, with only substitutions at D1.3 positions V(H)100 and V(H)101 greatly affecting binding to both ligands. Thus, the same protein may recognize different ligands in ways that are structurally similar yet energetically distinct.
机译：抗蛋清溶菌酶（HEL）抗体D1.3和HEL之间以及D1.3和抗D1.3抗体E5.2之间的复合物的晶体结构表明D1.3通过基本上是同一组结合位点残基[Fields，BA，Goldbaum，FA，Ysern，X.，Poljak，RJ，＆Mariuzza，RA（1995）Nature 374，739-742]，以探究各个残基对复杂的稳定化，在D1.3的结合位点引入单个丙氨酸取代，并使用表面等离振子共振检测，荧光猝灭滴定或沉降平衡测量其对HEL和E5.2亲和力的影响，结合的能量到HEL的水平仅受测试的13个接触残基中的3个支配（Delta G（突变）-Delta G（野生型）> 2.5 kcal / mol）：V（L）W92，V（H）D1C0和V（H） Y101。它们在界面的中心形成补丁，并被其表观贡献不明显（<1.5 kcal / mol）的残基包围。这与D1.3与E5.2的相互作用形成对比，在D5.2中，大多数接触残基（15个中的11个）在配体结合中起着重要作用（> 1.5 kcal / mol）。此外，即使D1.3以非常相似的方式接触HEL和E5.2，D1.3的功能上重要的残基对于两种相互作用也是不同的，仅在D1.3的位置V（H）100和V（H 101）极大地影响了与两个配体的结合。因此，相同的蛋白质可以以结构相似但能量上不同的方式识别不同的配体。

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