Volume 53, Issue 37 p. 9961
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Inside Back Cover: An Unusual Protein–Protein Interaction through Coupled Unfolding and Binding (Angew. Chem. Int. Ed. 37/2014)

Tae-Kyung Yu

Tae-Kyung Yu

Biomodulation Major, Department of Agricultural Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea)

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Seung-A Shin

Seung-A Shin

Biomodulation Major, Department of Agricultural Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea)

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Eun-Hee Kim

Eun-Hee Kim

Division of Magnetic Resonance, Korea Basic Science Institute, 16 Yeongudanji-Ro, Ochang, Chungbuk 363-883 (South Korea)

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Dr. Sunghyun Kim

Dr. Sunghyun Kim

KAIST Institute for the BioCentury, Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 291 Daehak-ro, Daejeon 305-701 (South Korea)

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Dr. Kyung-Seok Ryu

Dr. Kyung-Seok Ryu

Division of Magnetic Resonance, Korea Basic Science Institute, 16 Yeongudanji-Ro, Ochang, Chungbuk 363-883 (South Korea)

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Dr. Haekap Cheong

Dr. Haekap Cheong

Division of Magnetic Resonance, Korea Basic Science Institute, 16 Yeongudanji-Ro, Ochang, Chungbuk 363-883 (South Korea)

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Prof. Dr. Hee-Chul Ahn

Prof. Dr. Hee-Chul Ahn

Department of Pharmacy, Dongguk University-Seoul, Dongguk-ro 32, Ilsandong-gu, Goyang, Gyeonggi, 410-820 (South Korea)

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Prof. Dr. Sangyong Jon

Prof. Dr. Sangyong Jon

KAIST Institute for the BioCentury, Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 291 Daehak-ro, Daejeon 305-701 (South Korea)

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Prof. Dr. Jeong-Yong Suh

Corresponding Author

Prof. Dr. Jeong-Yong Suh

Biomodulation Major, Department of Agricultural Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea)

Biomodulation Major, Department of Agricultural Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea)Search for more papers by this author
First published: 07 July 2014

Graphical Abstract

Protein–protein interactions can involve the folding of a disordered region to form the binding interface. In their Communication on page 9784 ff., J. Y. Suh and co-workers report the opposite case, in which binding is accompanied by local unfolding. The structure of an engineered peptide bound to fibronectin extradomain B reveals coupled unfolding and binding through β-strand displacement. The unfolding exposes a hydrophobic surface that provides key interactions for the complex.

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