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2FY1

A dual mode of RNA recognition by the RBMY protein

Summary for 2FY1
Entry DOI10.2210/pdb2fy1/pdb
DescriptorS1A stem-loop RNA, RNA-binding motif protein, Y chromosome, family 1 member A1 (2 entities in total)
Functional Keywordsrna binding protein, protein-rna complex, rna stem-loop, structural protein-rna complex, structural protein/rna
Biological sourceHomo sapiens (human)
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Total number of polymer chains2
Total formula weight19524.69
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 citationSkrisovska, 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: 17318228
DOI: 10.1038/sj.embor.7400910
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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