Reconciliation of the X-ray and NMR structures of the thrombin-binding aptamer d(GGTTGGTGTGGTTGG)
Reconciliation of the X-ray and NMR structures of the thrombin-binding aptamer d(GGTTGGTGTGGTTGG)
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DOI：
10.1006/jmbi.1996.0097
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发表时间：
1996-03-01
影响因子：
5.6
通讯作者：
Yeates, TO
中科院分区：
文献类型：
--
作者：
Kelly, JA;Feigon, J;Yeates, TO
凝血酶结合适体d（GGTTGGTGTGGTTGG）是DNA寡核基家族中的一员，通过体外筛选鉴定其与凝血酶具有特异性和高亲和力。两组分别用NMR测定了溶液中的三级结构，同时报道了适体与凝血酶配合物的x射线晶体结构。在所有情况下，发现凝血酶结合适体折叠成包含两个平面鸟嘌呤四重奏为核心的结构。然而，由于这些中心碱基连接方式的不同，核磁共振和晶体结构具有根本不同的折叠模式。我们讨论了精炼晶体和溶液结构的区别，并表明核磁共振模型与x射线衍射数据是一致的。(C) 1996学术出版社有限公司
The thrombin-binding aptamer d(GGTTGGTGTGGTTGG) is one of a family of DNA oligonucleotldes that were identified by in vitro selection to bind specifically and with high affinity to thrombin. Two groups independently determined the tertiary structure in solution by NMR and at about the same time, the X-ray crystal structure of the aptamer in complex with thrombin was reported. In all cases, the thrombin-binding aptamer was found to fold into a structure containing two planar guanine quartets as its core. The NMR and crystal structures, however, have fundamentally different folding patterns owing to differences in the way these central bases are connected. We discuss the distinctions between the refined crystal and solution structures and show that the NMR model is consistent with the X-ray diffraction data. (C) 1996 Academic Press Limited