User:Dzmitry Mukha/sandbox1

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'''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''' 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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Human hnRNP A1 consists of 320 amino acids. N-terminal region is composed of 2 RNA recognition motifs (RRM) followed by highly flexible C-terminal glycine-rich region (45 % of glycine). The structure of disordered C-terminal region has not been resolved till now. <scene name='70/701439/Na_domain1/1'>RRM1</scene> and <scene name='70/701439/Na_binding_2/1'>RRM2</scene> (together span residues 1 to 196) form <scene name='70/701439/Na_binding_1/1'>unwinding protein 1 (UP1)</scene>.
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Human hnRNP A1 consists of 320 amino acids. N-terminal region is composed of 2 RNA recognition motifs (RRM) followed by highly flexible C-terminal glycine-rich region. The structure of disordered C-terminal region which contains 45 % of glycine in its sequence has not been resolved till now. However, a short peptide from C-terminal region (residues 315 – 341) is available in the structure of transportin bound to hnRNP A1 (2H4M). <scene name='70/701439/Na_domain1/1'>RRM1</scene> and <scene name='70/701439/Na_binding_2/1'>RRM2</scene> (together span residues 1 to 196) form <scene name='70/701439/Na_binding_1/1'>unwinding protein 1 (UP1)</scene>.
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The secondary structure of the RRM is characterized by a βαβαββαβ-fold in which the four b-strands make a relatively flat, anti-parallel β-sheet that forms most of the nucleic acid binding surface.
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The secondary structure of the RRM is characterized by a βαβαββαβ-fold in which the four β-strands make a flat 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 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>.
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== Binding ==
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== Conservative resudues ==
== Interaction between RRM domains ==
== Interaction between RRM domains ==
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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.
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== Structural highlights ==
 
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
 
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Myers, J.C., Moore, S.A., 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. (2003) J.BIOL.CHEM. 278: 42300-42306
 
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Myers, J.C., Shamoo, Y. Human UP1 as a model for understanding purine recognition in the family of proteins containing the RNA recognition motif (RRM). (2004) J.Mol.Biol. 342: 743-756
 
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Barraud, P., Allain, F.H. 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. (2013) J.Biomol.Nmr 55: 119-138
 
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 11:59, 5 May 2015

Nucleic acid binding mechanism of hnRNP A1

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. ↑ 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

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