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Inside Back Cover: An Unusual Protein–Protein Interaction through Coupled Unfolding and Binding (Angew. Chem. Int. Ed. 37/2014) 下载免费PDF全文
Tae‐Kyung Yu Seung‐A Shin Eun‐Hee Kim Dr. Sunghyun Kim Dr. Kyung‐Seok Ryu Dr. Haekap Cheong Prof. Dr. Hee‐Chul Ahn Prof. Dr. Sangyong Jon Prof. Dr. Jeong‐Yong Suh 《Angewandte Chemie (International ed. in English)》2014,53(37):9961-9961
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Tae‐Kyung Yu Seung‐A Shin Eun‐Hee Kim Dr. Sunghyun Kim Dr. Kyung‐Seok Ryu Dr. Haekap Cheong Prof. Dr. Hee‐Chul Ahn Prof. Dr. Sangyong Jon Prof. Dr. Jeong‐Yong Suh 《Angewandte Chemie (International ed. in English)》2014,53(37):9784-9787
Aptides, a novel class of high‐affinity peptides, recognize diverse molecular targets with high affinity and specificity. The solution structure of the aptide APT specifically bound to fibronectin extradomain B (EDB), which represents an unusual protein–protein interaction that involves coupled unfolding and binding, is reported. APT binding is accompanied by unfolding of the C‐terminal β strand of EDB, thereby permitting APT to interact with the freshly exposed hydrophobic interior surfaces of EDB. The β‐hairpin scaffold of APT drives the interaction by a β‐strand displacement mechanism, such that an intramolecular β sheet is replaced by an intermolecular β sheet. The unfolding of EDB perturbs the tight domain association between EDB and FN8 of fibronectin, thus highlighting its potential use as a scaffold that switches between stretched and bent conformations. 相似文献
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