4jlq
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of human Karyopherin-beta2 bound to the PY-NLS of Saccharomyces cerevisiae NAB2== | |
| - | + | <StructureSection load='4jlq' size='340' side='right' caption='[[4jlq]], [[Resolution|resolution]] 3.05Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4jlq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4h1k 4h1k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JLQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JLQ FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KPNB2, MIP1, TNPO1, TRN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), NAB2, YGL122C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4jlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jlq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jlq RCSB], [http://www.ebi.ac.uk/pdbsum/4jlq PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/TNPO1_HUMAN TNPO1_HUMAN]] Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Appears also to be involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Mediates nuclear import of ADAR/ADAR1 (isoform 5) in a RanGTP-dependent manner.<ref>PMID:8986607</ref> <ref>PMID:9687515</ref> <ref>PMID:11682607</ref> <ref>PMID:19124606</ref> [[http://www.uniprot.org/uniprot/NAB2_YEAST NAB2_YEAST]] This essential protein binds to polyadenylated RNA and single-stranded DNA. It may be involved not only in RNA processing but also in transcription regulation. Believed to associate directly with nascent RNA polymerase II transcripts and remain associated during subsequent nuclear RNA processing reactions. | [[http://www.uniprot.org/uniprot/TNPO1_HUMAN TNPO1_HUMAN]] Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Involved in nuclear import of M9-containing proteins. In vitro, binds directly to the M9 region of the heterogeneous nuclear ribonucleoproteins (hnRNP), A1 and A2 and mediates their nuclear import. Appears also to be involved in hnRNP A1/A2 nuclear export. Mediates the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor binding (BIB) domain of RPL23A. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones, and SRP19. In case of HIV-1 infection, binds and mediates the nuclear import of HIV-1 Rev. Mediates nuclear import of ADAR/ADAR1 (isoform 5) in a RanGTP-dependent manner.<ref>PMID:8986607</ref> <ref>PMID:9687515</ref> <ref>PMID:11682607</ref> <ref>PMID:19124606</ref> [[http://www.uniprot.org/uniprot/NAB2_YEAST NAB2_YEAST]] This essential protein binds to polyadenylated RNA and single-stranded DNA. It may be involved not only in RNA processing but also in transcription regulation. Believed to associate directly with nascent RNA polymerase II transcripts and remain associated during subsequent nuclear RNA processing reactions. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Import-Karyopherin or Importin proteins bind nuclear localization signals (NLSs) to mediate the import of proteins into the cell nucleus. Karyopherin beta2 or Kapbeta2, also known as Transportin, is a member of this transporter family responsible for the import of numerous RNA binding proteins. Kapbeta2 recognizes a targeting signal termed the PY-NLS that lies within its cargos to target them through the nuclear pore complex. The recognition of PY-NLS by Kapbeta2 is conserved throughout eukaryotes. Kap104, the Kapbeta2 homolog in Saccharomyces cerevisiae, recognizes PY-NLSs in cargos Nab2, Hrp1, and Tfg2. We have determined the crystal structure of Kapbeta2 bound to the PY-NLS of the mRNA processing protein Nab2 at 3.05-A resolution. A seven-residue segment of the PY-NLS of Nab2 is observed to bind Kapbeta2 in an extended conformation and occupies the same PY-NLS binding site observed in other Kapbeta2.PY-NLS structures. | ||
| - | + | Crystal structure of human Karyopherin beta2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2.,Soniat M, Sampathkumar P, Collett G, Gizzi AS, Banu RN, Bhosle RC, Chamala S, Chowdhury S, Fiser A, Glenn AS, Hammonds J, Hillerich B, Khafizov K, Love JD, Matikainen B, Seidel RD, Toro R, Rajesh Kumar P, Bonanno JB, Chook YM, Almo SC J Struct Funct Genomics. 2013 Jun;14(2):31-5. doi: 10.1007/s10969-013-9150-1., Epub 2013 Mar 28. PMID:23535894<ref>PMID:23535894</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | |||
| + | ==See Also== | ||
| + | *[[Importin|Importin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Saccharomyces cerevisiae s288c]] | [[Category: Saccharomyces cerevisiae s288c]] | ||
| - | [[Category: Almo, S C | + | [[Category: Almo, S C]] |
| - | [[Category: Chook, Y M | + | [[Category: Chook, Y M]] |
| - | [[Category: Gizzi, A | + | [[Category: Gizzi, A]] |
| - | [[Category: NPCXstals, Nucleocytoplasmic Transport:.a Target for Cellular Control | + | [[Category: NPCXstals, Nucleocytoplasmic Transport:.a Target for Cellular Control]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Rout, M P | + | [[Category: Rout, M P]] |
| - | [[Category: Sampathkumar, P | + | [[Category: Sampathkumar, P]] |
[[Category: Heat repeat]] | [[Category: Heat repeat]] | ||
[[Category: Importin]] | [[Category: Importin]] | ||
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[[Category: Proteintransport]] | [[Category: Proteintransport]] | ||
[[Category: Psi-biology]] | [[Category: Psi-biology]] | ||
| - | [[Category: Structural genomic]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
[[Category: Transportin]] | [[Category: Transportin]] | ||
Revision as of 19:09, 25 December 2014
Crystal structure of human Karyopherin-beta2 bound to the PY-NLS of Saccharomyces cerevisiae NAB2
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Categories: Homo sapiens | Saccharomyces cerevisiae s288c | Almo, S C | Chook, Y M | Gizzi, A | NPCXstals, Nucleocytoplasmic Transport:.a Target for Cellular Control | Structural genomic | Rout, M P | Sampathkumar, P | Heat repeat | Importin | Karyopherin | Nab2 | Nl | Nuclear import | Proteintransport | Psi-biology | Transport protein | Transportin
