NDLI: Crystal structure of human angiogenin with an engineered loop exhibits conformational flexibility at the functional regions of the molecule

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Crystal structure of human angiogenin with an engineered loop exhibits conformational flexibility at the functional regions of the molecule

Content Provider	Scilit
Author	Thiyagarajan, Nethaji Acharya, K. Ravi
Copyright Year	2012
Description	Journal: FEBS Open Bio ▸ A hybrid form (AEH) of human angiogenin (ANG) was created. ▸ The RI binding loop of ANG was substituted with the RI binding loop of EDN. ▸ Significant conformational changes were observed in the structure of AEH. ▸ Changes include the C-terminal segment and a putative cell binding domain of ANG. ▸ Binding of a chloride ion at the active site was observed
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668512/pdf
Ending Page	70
Page Count	6
Starting Page	65
ISSN	22115463
e-ISSN	22115463
DOI	10.1016/j.fob.2012.12.003
Journal	FEBS Open Bio
Issue Number	1
Volume Number	3
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2012-12-26
Access Restriction	Open
Subject Keyword	Journal: FEBS Open Bio Biochemistry and Molecular Biology Eosinophil Derived Neurotoxin Ribonuclease A Crystal Structure Protein Engineering Conformational Flexibility Rnase A, - Ribonuclease A Ang, - Human Angiogenin Edn -, Eosinophil Derived Neurotoxin Aeh -, Angiogenin–eosinophil Derived Neurotoxin Hybrid Ri -, Ribonuclease Inhibitor
Content Type	Text
Resource Type	Article
Subject	Biochemistry, Genetics and Molecular Biology

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