2014•Chemical CommunicationsRequires access

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

Kwon Joo Yeo, Eunha Hwang, Kyong-Mi Min, Jun-Goo Jee, Chung-Kyung Lee, Kwang Yeon Hwang, Young Ho Jeon, Soo‐Ik Chang, Hae‐Kap Cheong

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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.

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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.

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Available 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.

Key concepts: Angiogenin, Heparin, Chemistry, Dual (grammatical number), Mechanism (biology), Binding site, Biophysics, Biochemistry

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