Binding Interface Between C209 P4-P6 and Fab2. Fab2 binds to
C209 P4-P6 with an exceptionally large buried surface area (Fig.
4A), 1,316 Å2 (on the Fab side alone), which is almost twice as large
as that of most Fab–protein antigen interfaces (777135 Å2) (35).
Consistent with the extensive surface burial, residues from all six
CDRs and some scaffold residues form the interface (Fig. 4 and SI Fig. 11). Superposition of the variable domains reveals significant
differences in the main chain conformations of CDR-H3, L2 and
H2 compared with the parent (32) Fab-4D5, illustrating the conformational
plasticity of the hypervariable regions (Fig. 4B). Within
the Fab–RNA interface, CDR-H3 and L2 make direct contact with
both P5a and P5c stems and contribute most to the buried surface
area: 34% and 29%, respectively (Fig. 4C). This observation
suggests that CDR-H3 and L2 likely play significant roles in the
recognition of C209 P4-P6, even though L2 was not diversified in
the library
这篇论文里面是有插图的，括号里面的fig就是指里面的图片，没必要注意。我要求不高，能把大概意思说出来就行
结合C209 P4-P6和Fab2之间的接口。 Fab2裹
C209 P4-P6与一个特大的表面积(图埋。
4 A),1316安培(边独自厂),几乎是大两倍
最Fab-protein抗原的界面(777135安培)(35)。
一致与广泛的表面被埋葬,残留物6个
CDRs和一些脚手架残留形成界面(图4和图11)。叠加的变域揭示具有很重要的意义
主链构象差异的CDR-H3,二语
H2相比(32)Fab-4D5父母,阐述了构象
hypervariable可塑性的区域(图4 B)。 在
Fab-RNA的界面,CDR-H3和外语使直接接触
两P5a和P5c茎和影响为主埋表面
区:分别为34%和29%(图4 C)。这个观察
参考知识1
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