Issue 86, 2016, Issue in Progress
From the journal:

RSC Advances

The role of the KRSIK motif of human angiogenin in heparin and DNA binding†

Kwon Joo Yeo,‡ad   Jun-Goo Jee,‡b   Jin-Wan Park,a   Yu-Jin Lee,c   Kyoung-Seok Ryu,a   Byoung-Mog Kwon,c   Young Ho Jeon*d  and  Hae-Kap Cheong*a  

* Corresponding authors

a Protein Structure Group, Korea Basic Science Institute, 162 Yeongudanji-ro, Ochang, Chungbuk, Republic of Korea
E-mail: haekap@kbsi.re.kr

b College of Pharmacy, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 41566, Republic of Korea

c Korea Research Institute of Bioscience and Biotechnology, 125Gwahak-ro, Yuseong-gu, Daejeon, Republic of Korea

d College of Pharmacy, Korea University, 2511 Sejong-ro, Sejong, Republic of Korea
E-mail: yhjeon@korea.ac.kr

Abstract

The positively charged surface with a 50KRSIK54 motif is the main interaction site of hAng for both heparin and DNA binding, providing an insight into the potential role of the 50KRSIK54 motif for the internalization and promoter binding of hAng, which is essential for the regulation of angiogenesis.

Graphical abstract: The role of the KRSIK motif of human angiogenin in heparin and DNA binding

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Article information

DOI
https://doi.org/10.1039/C6RA14599J
Article type
Communication
Submitted
05 Jun 2016
Accepted
11 Aug 2016
First published
24 Aug 2016

RSC Adv., 2016,6, 82644-82647

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The role of the KRSIK motif of human angiogenin in heparin and DNA binding

K. J. Yeo, J. Jee, J. Park, Y. Lee, K. Ryu, B. Kwon, Y. H. Jeon and H. Cheong, RSC Adv., 2016, 6, 82644 DOI: 10.1039/C6RA14599J

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