英语翻译CDR-H3 resides in the center of the P5a/P5c helical interface atthe three-helix junction (Fig.5A).Residues Gly-98,Ser-100,andThr100a interact with the wide and shallowminor groove of P5c viadirect H bonds,and Tyr-102 contacts P5a by H bon

英语翻译CDR-H3 resides in the center of the P5a/P5c helical interface atthe three-helix junction (Fig.5A).Residues Gly-98,Ser-100,andThr100a interact with the wide and shallowminor groove of P5c viadirect H bonds,and Tyr-102 contacts P5a by H bon
英语翻译
CDR-H3 resides in the center of the P5a/P5c helical interface at
the three-helix junction (Fig.5A).Residues Gly-98,Ser-100,and
Thr100a interact with the wide and shallowminor groove of P5c via
direct H bonds,and Tyr-102 contacts P5a by H bonding to U131 in
the minor groove.Several CDR-H3 residues form a pocket (Fig.
5B) that encloses U130,the bulged uridine in P5a,and they use a
variety of molecular strategies to interact with U130.Arg-94,
Ala-96,Asp-101,and Gly100c form direct H bonds to the uracil
base and sugar ring,whereas the side chains of Ala-96 and Met-99
embrace the nucleotide with nonpolar contacts.Tyr100b stacks
perpendicularly with the base,and Arg-94 forms an N-O bridgetype
of ion pair with the adjacent phosphate (36).Interestingly,
although Arg-95 was selected from the library,it makes no interaction
with the RNA in the structure; instead,its side chain points
away from theRNAand makes hydrogen bonding interactions with
the backbone carbonyl groups of Tyr100b and Met-99,possibly
stabilizing the CDR-H3 loop conformation.
CDR-L2 loop residues (defined as residues 50–56) (37) and the
flanking framework residues interact extensively with RNA,mainly
in the P5a minor groove.Residues Ser-56,Gly-57,and Ser-60 form
direct H bonds to the 3\2 strand of P5a,across from U130 near the
hinge region (Fig.5A).A possible long-range ion pair between
Arg-61 and the phosphate moiety of C197 may stabilize this
interaction.Direct H bonding between Ser-50 and the U167
phosphate links CDR-L2 to P5c,making L2 another CDR that
binds both helical stems.Tyr-49 and Tyr-55 stack perpendicularly
with U130 from the nonpolar side to seal the U130-binding pocket
generated by CDR-H3 (Fig.5B).Three water molecules organized
by the four tyrosine residues surrounding U130 interact with the
sugar–phosphate moiety,which may further strengthen the RNAFab
interaction at the nonpolar interface of the U130 binding
pocket (Fig.5C).
我需要大致了解一下它的意思,不用太准确,大概意思说一下就行

英语翻译CDR-H3 resides in the center of the P5a/P5c helical interface atthe three-helix junction (Fig.5A).Residues Gly-98,Ser-100,andThr100a interact with the wide and shallowminor groove of P5c viadirect H bonds,and Tyr-102 contacts P5a by H bon
CDR-H3居住在中心的P5a / P5c螺旋接口
three-helix交界处的(图5).残留Gly - 98,萨尔- 100,
Thr100a交互槽宽,shallowminor P5c通过
直接H债券,和接触P5a钟- 102通过催眠与U131
小槽.几个CDR-H3残留(图形成一个口袋里.
5 B)U130封装,尿在P5a胀得鼓鼓的,他们会使用
各种分子的策略与U130互动.高温- 94,
Ala - 96,Asp - 101,Gly100c债券的形式直接H尿嘧啶
基地和糖环,而基侧链的Ala - 96,并会见了99 -
拥抱核苷酸与非极性接触.Tyr100b堆栈
直立地与基地,来形成一个N-O bridgetype - 94
与相邻的离子对磷酸盐(36).有趣的是,
尽管高温- 95年本院图书馆,它使没有交互作用
与RNA结构;相反的,其侧链的分
远离theRNAand使氢键相互作用
羰基化合物的骨干,并会见了Tyr100b - 99,可能
CDR-H3循环稳定构象.
CDR-L2回路残留(定义为残留50-56)(37)和
残留在框架广泛地互动RNA、为主
在P5a小槽.Ser-56残留物,Gly-57,Ser-60形式
直接到3 H债券的一条P5a,跨过U130靠近
铰链区(图5).一个可能的远程离子对之间
高温- 61和磷酸盐半族的C197可能保持稳定
互动.Ser-50直接H和U167之间的融洽
链接到P5c CDR-L2磷酸盐,使L2另一个CDR
将两个螺旋杆.Tyr-49堆栈和Tyr-55直立地
从非极性与U130侧封U130-binding口袋里
所产生的CDR-H3(图5 B).组织三个水分子
由四个酪氨酸残U130交互周围
sugar-phosphate半族,这可能进一步加强RNAFab
在非极性相互作用的界面,该U130约束力
口袋(图5 C).
以上是用有道在线翻译的,越看越别扭,