Issue 85, 2014
From the journal:

Chemical Communications

The dual binding site of angiogenin and its inhibition mechanism: the crystal structure of the rat angiogenin–heparin complex†

Kwon Joo Yeo,ab   Eunha Hwang,ab   Kyong-Mi Min,c   Jun-Goo Jee,d   Chung-Kyung Lee,a   Kwang Yeon Hwang,b   Young Ho Jeon,e   Soo-Ik Chang*c  and  Hae-Kap Cheong*a  

* Corresponding authors

a Division of Magnetic Resonance, Korea Basic Science Institute (KBSI), 162 Yeongudanji-ro, Ochang, Chungbuk 363-883, Republic of Korea
E-mail: haekap@kbsi.re.kr

b Division of Biotechnology, College of Life Sciences & Biotechnology, Korea University, Seoul, Republic of Korea

c Department of Biochemistry, Chungbuk National University, 52 Naesudong-ro, Seowon-gu, Cheongju, Chungbuk 362-763, Republic of Korea
E-mail: sichang@chungbuk.ac.kr

d Research Institute of Pharmaceutical Sciences, College of Pharmacy, Kyungpook National University, 80 Daehak-ro, Buk-gu, Daegu 702-701, Republic of Korea

e College of Pharmacy, Korea University, Sejong-ro, Sejong, Republic of Korea

Abstract

The heparin complex of rat angiogenin revealed that a heparin strand is fitted into a positively charged groove formed by the dual binding site of rat angiogenin, suggesting that cell adhesion to angiogenin is facilitated by its interaction with substrates on the cell surface and can be inhibited by heparin.

Graphical abstract: The dual binding site of angiogenin and its inhibition mechanism: the crystal structure of the rat angiogenin–heparin complex

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Article information

DOI
https://doi.org/10.1039/C4CC05175K
Article type
Communication
Submitted
05 Jul 2014
Accepted
22 Aug 2014
First published
02 Sep 2014

Chem. Commun., 2014,50, 12966-12969

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The dual binding site of angiogenin and its inhibition mechanism: the crystal structure of the rat angiogenin–heparin complex

K. J. Yeo, E. Hwang, K. Min, J. Jee, C. Lee, K. Y. Hwang, Y. H. Jeon, S. Chang and H. Cheong, Chem. Commun., 2014, 50, 12966 DOI: 10.1039/C4CC05175K

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