2FY1
A dual mode of RNA recognition by the RBMY protein
Summary for 2FY1
| Entry DOI | 10.2210/pdb2fy1/pdb |
| Descriptor | S1A stem-loop RNA, RNA-binding motif protein, Y chromosome, family 1 member A1 (2 entities in total) |
| Functional Keywords | rna binding protein, protein-rna complex, rna stem-loop, structural protein-rna complex, structural protein/rna |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 19524.69 |
| Authors | Skrisovska, L.,Bourgois, C.,Stefl, R.,Kister, L.,Wenter, P.,Elliot, D.,Stevenin, J.,Allain, F.H.T. (deposition date: 2006-02-07, release date: 2007-02-06, Last modification date: 2024-05-01) |
| Primary citation | Skrisovska, L.,Bourgeois, C.F.,Stefl, R.,Grellscheid, S.N.,Kister, L.,Wenter, P.,Elliott, D.J.,Stevenin, J.,Allain, F.H. The testis-specific human protein RBMY recognizes RNA through a novel mode of interaction. EMBO Rep., 8:372-379, 2007 Cited by PubMed Abstract: The RBMY (RNA-binding motif gene on Y chromosome) protein encoded by the human Y chromosome is important for normal sperm development. Although its precise molecular RNA targets are unknown at present, it is suggested that human RBMY (hRBMY) participates in splicing in the testis. Using systematic evolution of ligands by exponential enrichment, we found that RNA stem-loops capped by a C(A)/(U)CAA pentaloop are high-affinity binding targets for hRBMY. Subsequent nuclear magnetic resonance structural determination of the hRBMY RNA recognition motif (RRM) in complex with a high-affinity target showed two distinct modes of RNA recognition. First, the RRM beta-sheet surface binds to the RNA loop in a sequence-specific fashion. Second, the beta2-beta3 loop of the hRBMY inserts into the major groove of the RNA stem. The first binding mode might be conserved in the paralogous protein heterogeneous nuclear RNP G, whereas the second mode of binding is found only in hRBMY. This structural difference could be at the origin of the function of RBMY in spermatogenesis. PubMed: 17318228DOI: 10.1038/sj.embor.7400910 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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