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3SMZ

Human raver1 RRM1-3 domains (residues 39-320)

Summary for 3SMZ
Entry DOI10.2210/pdb3smz/pdb
Related3h2u 3h2v
DescriptorRibonucleoprotein PTB-binding 1, SULFATE ION (3 entities in total)
Functional Keywordsrna binding, ribonucleoprotein, rna recognition motif, vinculin, alpha-actinin, nucleus, rna binding protein
Biological sourceHomo sapiens (human)
Cellular locationNucleus (By similarity): Q8IY67
Total number of polymer chains1
Total formula weight31780.08
Authors
Rangarajan, E.S.,Lee, J.H.,Izard, T. (deposition date: 2011-06-28, release date: 2011-08-10, Last modification date: 2024-11-20)
Primary citationRangarajan, E.S.,Lee, J.H.,Izard, T.
Apo raver1 structure reveals distinct RRM domain orientations.
Protein Sci., 20:1464-1470, 2011
Cited by
PubMed Abstract: Raver1 is a multifunctional protein that modulates both alternative splicing and focal adhesion assembly by binding to the nucleoplasmic splicing repressor polypyrimidine tract protein (PTB) or to the cytoskeletal proteins vinculin and α-actinin. The amino-terminal region of raver1 has three RNA recognition motif (RRM1, RRM2, and RRM3) domains, and RRM1 interacts with the vinculin tail (Vt) domain and vinculin mRNA. We previously determined the crystal structure of the raver1 RRM1-3 domains in complex with Vt at 2.75 Å resolution. Here, we report crystal structure of the unbound raver1 RRM1-3 domains at 2 Å resolution. The apo structure reveals that a bound sulfate ion disrupts an electrostatic interaction between the RRM1 and RRM2 domains, triggering a large relative domain movement of over 30°. Superposition with other RNA-bound RRM structures places the sulfate ion near the superposed RNA phosphate group suggesting that this is the raver1 RNA binding site. While several single and some tandem RRM domain structures have been described, to the best of our knowledge, this is the second report of a three-tandem RRM domain structure.
PubMed: 21633983
DOI: 10.1002/pro.664
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.99 Å)
Structure validation

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