Supplemental Information Protein-RNA and Protein-Protein Recognition by Dual KH 1 / 2 Domains of the Neuronal Splicing Factor Nova-1
Supplemental Information Protein-RNA and Protein-Protein Recognition by Dual KH 1 / 2 Domains of the Neuronal Splicing Factor Nova-1
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发表时间：
2011
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通讯作者：
M. Teplova;L. Malinina;J. Darnell;Jikui Song;Min Lu;R. Abagyan;K. Musunuru;A. Teplov;S. Burley;R. Darnell;D. Patel
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作者：
M. Teplova;L. Malinina;J. Darnell;Jikui Song;Min Lu;R. Abagyan;K. Musunuru;A. Teplov;S. Burley;R. Darnell;D. Patel
补充结果I型和II型复合体大多数Kh1-Kh2和Kh1-RNA界面以及Kh2-Kh2接触在I型(G2.C24对)和II型(Bru·A24对)复合体的结构上相似。一个不同之处是G12在两个复合体中的相对位置，因为不同的晶体接触与晶格中RNA发夹环的头尾对齐有关(图S1a和S1b)。此外，如上所述，在两种类型的络合物中，Lys40和Lys43的侧链与C10和C16的基边表现出不同的相互作用。
SUPPLEMENTAL RESULTS Type I and Type II Complexes The majority of the KH1-KH2 and KH1-RNA interfaces, as well as KH2-KH2 contacts are similar in the structures of the type I (G2•C24 pair) and type II (BrU•A24 pair) complexes. One difference is the relative positioning of G12 in the two complexes due to different crystal contacts associated with the head-to-tail alignment of RNA hairpin loops in the crystal lattice (Figures S1A and S1B). In addition, as described above, the side chains of Lys40 and Lys43 exhibit different interactions with the base edge of C10 and C16 in the two types of complexes.