The role of the KRSIK motif of human angiogenin in heparin and DNA binding
- Authors
- Yeo, Kwon Joo; Jee, Jun-Goo; Park, Jin-Wan; Lee, Yu-Jin; Ryu, Kyoung-Seok; Kwon, Byoung-Mog; Jeon, Young Ho; Cheong, Hae-Kap
- Issue Date
- 2016
- Publisher
- ROYAL SOC CHEMISTRY
- Citation
- RSC ADVANCES, v.6, no.86, pp.82644 - 82647
- Indexed
- SCIE
SCOPUS
- Journal Title
- RSC ADVANCES
- Volume
- 6
- Number
- 86
- Start Page
- 82644
- End Page
- 82647
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/90274
- DOI
- 10.1039/c6ra14599j
- ISSN
- 2046-2069
- Abstract
- The positively charged surface with a (KRSIK54)-K-50 motif is the main interaction site of hAng for both heparin and DNA binding, providing an insight into the potential role of the (KRSIK54)-K-50 motif for the internalization and promoter binding of hAng, which is essential for the regulation of angiogenesis.
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- There are no files associated with this item.
- Appears in
Collections - College of Pharmacy > Department of Pharmaceutical Science > 1. Journal Articles
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