+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDAR4 |
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Sample | PTB full
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Function / homology | Function and homology information negative regulation of muscle cell differentiation / poly-pyrimidine tract binding / IRES-dependent viral translational initiation / positive regulation of calcineurin-NFAT signaling cascade / pre-mRNA binding / negative regulation of RNA splicing / FGFR2 alternative splicing / regulation of cell differentiation / regulation of alternative mRNA splicing, via spliceosome / negative regulation of mRNA splicing, via spliceosome ...negative regulation of muscle cell differentiation / poly-pyrimidine tract binding / IRES-dependent viral translational initiation / positive regulation of calcineurin-NFAT signaling cascade / pre-mRNA binding / negative regulation of RNA splicing / FGFR2 alternative splicing / regulation of cell differentiation / regulation of alternative mRNA splicing, via spliceosome / negative regulation of mRNA splicing, via spliceosome / regulation of RNA splicing / Processing of Capped Intron-Containing Pre-mRNA / positive regulation of protein dephosphorylation / mRNA Splicing - Major Pathway / RNA splicing / mRNA processing / mRNA binding / nucleolus / RNA binding / extracellular exosome / nucleoplasm / membrane / nucleus Similarity search - Function |
Biological species | Homo sapiens (human) |
Citation | Journal: Structure / Year: 2006 Title: Conformation of polypyrimidine tract binding protein in solution. Authors: Maxim V Petoukhov / Tom P Monie / Frédéric H-T Allain / Stephen Matthews / Stephen Curry / Dmitri I Svergun / 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. |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Data source
SASBDB page | SASDAR4 |
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-Related structure data
Similar structure data |
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-External links
Related items in Molecule of the Month |
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-Models
Model #76 | Type: mix / Software: Bunch / Radius of dummy atoms: 1.90 A / Chi-square value: 1.1664 Search similar-shape structures of this assembly by Omokage search (details) |
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-Sample
Sample | Name: PTB full / Sample MW: 57.22 kDa / Specimen concentration: 6.40-20.40 |
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Buffer | Name: 25 mM Tris / pH: 7.2 / Composition: 100 mM NaCl, 5.0 mM DTT |
Entity #65 | Type: protein / Description: Polypyrimidine tract-binding protein 1 / Formula weight: 57.22 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P26599 Sequence: MDGIVPDIAV GTKRGSDELF STCVTNGPFI MSSNSASAAN GNDSKKFKGD SRSAGVPSRV IHIRKLPIDV TEGEVISLGL PFGKVTNLLM LKGKNQAFIE MNTEEAANTM VNYYTSVTPV LRGQPIYIQF SNHKELKTDS SPNQARAQAA LQAVNSVQSG NLALAASAAA ...Sequence: MDGIVPDIAV GTKRGSDELF STCVTNGPFI MSSNSASAAN GNDSKKFKGD SRSAGVPSRV IHIRKLPIDV TEGEVISLGL PFGKVTNLLM LKGKNQAFIE MNTEEAANTM VNYYTSVTPV LRGQPIYIQF SNHKELKTDS SPNQARAQAA LQAVNSVQSG NLALAASAAA VDAGMAMAGQ SPVLRIIVEN LFYPVTLDVL HQIFSKFGTV LKIITFTKNN QFQALLQYAD PVSAQHAKLS LDGQNIYNAC CTLRIDFSKL TSLNVKYNND KSRDYTRPDL PSGDSQPSLD QTMAAAFGLS VPNVHGALAP LAIPSAAAAA AAAGRIAIPG LAGAGNSVLL VSNLNPERVT PQSLFILFGV YGDVQRVKIL FNKKENALVQ MADGNQAQLA MSHLNGHKLH GKPIRITLSK HQNVQLPREG QEDQGLTKDY GNSPLHRFKK PGSKNFQNIF PPSATLHLSN IPPSVSEEDL KVLFSSNGGV VKGFKFFQKD RKMALIQMGS VEEAVQALID LHNHDLGENH HLRVSFSKST I |
-Experimental information
Beam | Instrument name: DORIS III X33 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron | ||||||||||||||||||
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Detector | Name: 1D Gas detector | ||||||||||||||||||
Scan | Title: PTB full / Measurement date: Feb 11, 2004 / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 4.6 / Number of points: 355 /
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Result | Experimental MW: 60 kDa / Type of curve: merged
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