8AF0
Crystal structure of human angiogenin and RNA duplex
Summary for 8AF0
| Entry DOI | 10.2210/pdb8af0/pdb |
| Descriptor | RNA (5'-R(*GP*CP*CP*CP*GP*CP*CP*UP*GP*UP*CP*AP*CP*GP*CP*GP*GP*GP*C)-3'), Angiogenin, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | ribonuclease, rna duplex, rnase a-like, rna binding protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 40691.62 |
| Authors | Sievers, K.,Ficner, R. (deposition date: 2022-07-15, release date: 2022-09-14, Last modification date: 2024-11-06) |
| Primary citation | Sievers, K.,Ficner, R. Structure of angiogenin dimer bound to double-stranded RNA. Acta Crystallogr.,Sect.F, 78:330-337, 2022 Cited by PubMed Abstract: Angiogenin is an unusual member of the RNase A family and is of great interest in multiple pathological contexts. Although it has been assigned various regulatory roles, its core catalytic function is that of an RNA endonuclease. However, its catalytic efficiency is comparatively low and this has been linked to a unique C-terminal helix which partially blocks its RNA-binding site. Assuming that binding to its RNA substrate could trigger a conformational rearrangement, much speculation has arisen on the topic of the interaction of angiogenin with RNA. To date, no structural data on angiogenin-RNA interactions have been available. Here, the structure of angiogenin bound to a double-stranded RNA duplex is reported. The RNA does not reach the active site of angiogenin and no structural arrangement of the C-terminal domain is observed. However, angiogenin forms a previously unobserved crystallographic dimer that makes several backbone interactions with the major and minor grooves of the RNA double helix. PubMed: 36048083DOI: 10.1107/S2053230X22008317 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.43 Å) |
Structure validation
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