User:Dzmitry Mukha/sandbox1
From Proteopedia
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== Nucleic acid binding mechanism of hnRNP A1 == | == Nucleic acid binding mechanism of hnRNP A1 == | ||
| - | '''hnRNP A1''' is a member of A/B subfamily of heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). hnRNP A1 is involved in the packaging of premature mRNA into hnRNP particles and transport of poly(A) mRNA from the nucleus to the cytoplasm. hnRNP A1 has been characterized as a component of protein complexes bound to premature mRNA (hnRNP complexes). hnRNP A1 is one of the most abundant and best-characterized components of hnRNP complexes. Human hnRNP functions also in telomere length regulation and miRNA biogenesis. It may play a role in the replication of RNA viruses. | + | '''hnRNP A1''' (alternative gene names: ALS19, ALS20, HNRPA1, IBMPFD3, HNRPA1L3) is a member of A/B subfamily of heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). hnRNP A1 is involved in the packaging of premature mRNA into hnRNP particles and transport of poly(A) mRNA from the nucleus to the cytoplasm. hnRNP A1 has been characterized as a component of protein complexes bound to premature mRNA (hnRNP complexes). hnRNP A1 is one of the most abundant and best-characterized components of hnRNP complexes. Human hnRNP functions also in telomere length regulation and miRNA biogenesis. It may play a role in the replication of RNA viruses. |
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The secondary structure of the RRM is characterized by a βαβαββαβ-fold in which the four β-strands make an anti-parallel β-sheet that forms most of the nucleic acid binding surface. | The secondary structure of the RRM is characterized by a βαβαββαβ-fold in which the four β-strands make an anti-parallel β-sheet that forms most of the nucleic acid binding surface. | ||
| - | To date, several crystal structures of UP1 have been solved both in their free form and bound to repeats of telomeric DNA fragments. NMR structure of hnRNP A1 RRM domains was determined using a segmental labeling strategy <ref>PMID 23247503</ref>. | + | To date, several [[#Structures|crystal structures]] of UP1 have been solved both in their free form and bound to repeats of telomeric DNA fragments <ref>PMID 9115444</ref><ref>PMID 11917013</ref><ref>PMID 10323862</ref><ref>PMID 12904298</ref><ref>PMID 15342234</ref>. NMR structure of hnRNP A1 RRM domains was determined using a segmental labeling strategy <ref>PMID 23247503</ref>. |
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| + | === Post-translational modifications === | ||
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</StructureSection> | </StructureSection> | ||
| - | == Binding == | + | == Binding mechanism == |
== Conservative residues == | == Conservative residues == | ||
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== Interaction between RRM domains == | == Interaction between RRM domains == | ||
| - | Two RRMs are interaction with one another via two Arg-Asp salt bridges. The interactions between domains of UP1 is quite | + | Two RRMs are interaction with one another via two Arg-Asp salt bridges. The interactions between domains of UP1 is quite weak, since the orientation of the two RRMs can be influenced by nucleic acid binding or by contacts with neighboring molecules in the crystal lattice. |
In the solution structure of free UP1, the two Arg-Asp salt bridges are conserved at the interface between RRM1 and RRM2. | In the solution structure of free UP1, the two Arg-Asp salt bridges are conserved at the interface between RRM1 and RRM2. | ||
| - | == | + | == Protein-protein interactions == |
| + | |||
| + | == Medical implications == | ||
| + | |||
| + | == Structures == | ||
| + | === X-ray === | ||
| + | * [[1ha1]] | ||
| + | * [[1l3k]] | ||
| + | * [[1pgz]] | ||
| + | * [[1po6]] | ||
| + | * [[1u1k]] | ||
| + | * [[1u1l]] | ||
| + | * [[1u1m]] | ||
| + | * [[1u1n]] | ||
| + | * [[1u1o]] | ||
| + | * [[1u1p]] | ||
| + | * [[1u1q]] | ||
| + | * [[1u1r]] | ||
| + | * [[1up1]] | ||
| + | * [[2h4m]] | ||
| + | * [[2up1]] | ||
| + | |||
| + | === Solution NMR === | ||
| + | * [[2lyv]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| + | |||
| + | [[Category:Transcription|Transcription]] | ||
| + | [[Category:Rna processing |RNA Processing]] | ||
Revision as of 21:37, 18 May 2015
Nucleic acid binding mechanism of hnRNP A1
hnRNP A1 (alternative gene names: ALS19, ALS20, HNRPA1, IBMPFD3, HNRPA1L3) is a member of A/B subfamily of heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). hnRNP A1 is involved in the packaging of premature mRNA into hnRNP particles and transport of poly(A) mRNA from the nucleus to the cytoplasm. hnRNP A1 has been characterized as a component of protein complexes bound to premature mRNA (hnRNP complexes). hnRNP A1 is one of the most abundant and best-characterized components of hnRNP complexes. Human hnRNP functions also in telomere length regulation and miRNA biogenesis. It may play a role in the replication of RNA viruses.
Contents |
Structure overview
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Binding mechanism
Conservative residues
Interaction between RRM domains
Two RRMs are interaction with one another via two Arg-Asp salt bridges. The interactions between domains of UP1 is quite weak, since the orientation of the two RRMs can be influenced by nucleic acid binding or by contacts with neighboring molecules in the crystal lattice.
In the solution structure of free UP1, the two Arg-Asp salt bridges are conserved at the interface between RRM1 and RRM2.
Protein-protein interactions
Medical implications
Structures
X-ray
Solution NMR
References
- ↑ Xu RM, Jokhan L, Cheng X, Mayeda A, Krainer AR. Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs. Structure. 1997 Apr 15;5(4):559-70. PMID:9115444
- ↑ Vitali J, Ding J, Jiang J, Zhang Y, Krainer AR, Xu RM. Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1. Nucleic Acids Res. 2002 Apr 1;30(7):1531-8. PMID:11917013
- ↑ Ding J, Hayashi MK, Zhang Y, Manche L, Krainer AR, Xu RM. Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. Genes Dev. 1999 May 1;13(9):1102-15. PMID:10323862
- ↑ Myers JC, Moore SA, Shamoo Y. Structure-based incorporation of 6-methyl-8-(2-deoxy-beta-ribofuranosyl)isoxanthopteridine into the human telomeric repeat DNA as a probe for UP1 binding and destabilization of G-tetrad structures. J Biol Chem. 2003 Oct 24;278(43):42300-6. Epub 2003 Aug 6. PMID:12904298 doi:http://dx.doi.org/10.1074/jbc.M306147200
- ↑ Myers JC, Shamoo Y. Human UP1 as a model for understanding purine recognition in the family of proteins containing the RNA recognition motif (RRM). J Mol Biol. 2004 Sep 17;342(3):743-56. PMID:15342234 doi:10.1016/j.jmb.2004.07.029
- ↑ Barraud P, Allain FH. Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology. J Biomol NMR. 2012 Dec 18. PMID:23247503 doi:http://dx.doi.org/10.1007/s10858-012-9696-4
