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| Title | Conformation of polypyrimidine tract binding protein in solution. |
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| Journal, issue, pages | Structure, Vol. 14, Issue 6, Page 1021-1027, Year 2006 |
| Publish date | Aug 11, 2006 |
 Authors | Maxim V Petoukhov / Tom P Monie / Frédéric H-T Allain / Stephen Matthews / Stephen Curry / Dmitri I Svergun /  |
| PubMed Abstract | The polypyrimidine tract binding protein (PTB) is an RNA binding protein that normally functions as a regulator of alternative splicing but can also be recruited to stimulate translation initiation ...The polypyrimidine tract binding protein (PTB) is an RNA binding protein that normally functions as a regulator of alternative splicing but can also be recruited to stimulate translation initiation by certain picornaviruses. High-resolution structures of the four RNA recognition motifs (RRMs) that make up PTB have previously been determined by NMR. Here, we have used small-angle X-ray scattering to determine the low-resolution structure of the entire protein. Scattering patterns from full-length PTB and deletion mutants containing all possible sequential combinations of the RRMs were collected. All constructs were found to be monomeric in solution. Ab initio analysis and rigid-body modeling utilizing the high-resolution models of the RRMs yielded a consistent low-resolution model of the spatial organization of domains in PTB. Domains 3 and 4 were found to be in close contact, whereas domains 2 and especially 1 had loose contacts with the rest of the protein. |
 External links | Structure / PubMed:16765895 |
| Methods | SAS (X-ray synchrotron) |
| Structure data |  SASDAR4: |
| Source |
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Homo sapiens (human)