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| - | [[Image:1fjd.gif|left|200px]] | |
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| - | <!-- | + | ==HUMAN PARVULIN-LIKE PEPTIDYL PROLYL CIS/TRANS ISOMERASE, HPAR14== |
| - | The line below this paragraph, containing "STRUCTURE_1fjd", creates the "Structure Box" on the page.
| + | <StructureSection load='1fjd' size='340' side='right'caption='[[1fjd]]' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1fjd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FJD FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display. | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | -->
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fjd OCA], [https://pdbe.org/1fjd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fjd RCSB], [https://www.ebi.ac.uk/pdbsum/1fjd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fjd ProSAT], [https://www.topsan.org/Proteins/RSGI/1fjd TOPSAN]</span></td></tr> |
| - | {{STRUCTURE_1fjd| PDB=1fjd | SCENE= }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PIN4_HUMAN PIN4_HUMAN] Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.<ref>PMID:19369196</ref> Isoform 2 binds to double-stranded DNA.<ref>PMID:19369196</ref> |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/1fjd_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fjd ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | The hPar14 protein is a peptidyl prolyl cis/trans isomerase and is a human parvulin homologue. The hPar14 protein shows about 30 % sequence identity with the other human parvulin homologue, hPin1. Here, the solution structure of hPar14 was determined by nuclear magnetic resonance spectroscopy. The N-terminal 35 residues preceding the peptidyl prolyl isomerase domain of hPar14 are unstructured, whereas hPin1 possesses the WW domain at its N terminus. The fold of residues 36-131 of hPar14, which comprises a four-stranded beta-sheet and three alpha-helices, is superimposable onto that of the peptidyl prolyl isomerase domain of hPin1. To investigate the interaction of hPar14 with a substrate, the backbone chemical-shift changes of hPar14 were monitored during titration with a tetra peptide. Met90, Val91, and Phe94 around the N terminus of alpha3 showed large chemical-shift changes. These residues form a hydrophobic patch on the molecular surface of hPar14. Two of these residues are conserved and have been shown to interact with the proline residue of the substrate in hPin1. On the other hand, hPar14 lacks the hPin1 positively charged residues (Lys63, Arg68, and Arg69), which determine the substrate specificity of hPin1 by interacting with phosphorylated Ser or Thr preceding the substrate Pro, and exhibits a different structure in the corresponding region. Therefore, the mechanism determining the substrate specificity seems to be different between hPar14 and hPin1. |
| | | | |
| - | '''HUMAN PARVULIN-LIKE PEPTIDYL PROLYL CIS/TRANS ISOMERASE, HPAR14'''
| + | Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14.,Terada T, Shirouzu M, Fukumori Y, Fujimori F, Ito Y, Kigawa T, Yokoyama S, Uchida T J Mol Biol. 2001 Jan 26;305(4):917-26. PMID:11162102<ref>PMID:11162102</ref> |
| - | | + | |
| - | | + | |
| - | ==Overview==
| + | |
| - | The hPar14 protein is a peptidyl prolyl cis/trans isomerase and is a human parvulin homologue. The hPar14 protein shows about 30 % sequence identity with the other human parvulin homologue, hPin1. Here, the solution structure of hPar14 was determined by nuclear magnetic resonance spectroscopy. The N-terminal 35 residues preceding the peptidyl prolyl isomerase domain of hPar14 are unstructured, whereas hPin1 possesses the WW domain at its N terminus. The fold of residues 36-131 of hPar14, which comprises a four-stranded beta-sheet and three alpha-helices, is superimposable onto that of the peptidyl prolyl isomerase domain of hPin1. To investigate the interaction of hPar14 with a substrate, the backbone chemical-shift changes of hPar14 were monitored during titration with a tetra peptide. Met90, Val91, and Phe94 around the N terminus of alpha3 showed large chemical-shift changes. These residues form a hydrophobic patch on the molecular surface of hPar14. Two of these residues are conserved and have been shown to interact with the proline residue of the substrate in hPin1. On the other hand, hPar14 lacks the hPin1 positively charged residues (Lys63, Arg68, and Arg69), which determine the substrate specificity of hPin1 by interacting with phosphorylated Ser or Thr preceding the substrate Pro, and exhibits a different structure in the corresponding region. Therefore, the mechanism determining the substrate specificity seems to be different between hPar14 and hPin1.
| + | |
| | | | |
| - | ==About this Structure==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 1FJD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJD OCA].
| + | </div> |
| | + | <div class="pdbe-citations 1fjd" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Reference== | + | ==See Also== |
| - | Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14., Terada T, Shirouzu M, Fukumori Y, Fujimori F, Ito Y, Kigawa T, Yokoyama S, Uchida T, J Mol Biol. 2001 Jan 26;305(4):917-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11162102 11162102]
| + | *[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]] |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Fujimori, F.]] | + | [[Category: Fujimori F]] |
| - | [[Category: Fukumori, Y.]] | + | [[Category: Fukumori Y]] |
| - | [[Category: Ito, Y.]] | + | [[Category: Ito Y]] |
| - | [[Category: Kigawa, T.]] | + | [[Category: Kigawa T]] |
| - | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
| + | [[Category: Shirouzu M]] |
| - | [[Category: Shirouzu, M.]] | + | [[Category: Terada T]] |
| - | [[Category: Terada, T.]] | + | [[Category: Uchida T]] |
| - | [[Category: Uchida, T.]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama, S.]] | + | |
| - | [[Category: Parvulin]]
| + | |
| - | [[Category: Peptidyl prolyl cis/trans isomerase]]
| + | |
| - | [[Category: Riken structural genomics/proteomics initiative]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:23:51 2008''
| + | |
| Structural highlights
Function
PIN4_HUMAN Isoform 1 is involved as a ribosomal RNA processing factor in ribosome biogenesis. Binds to tightly bent AT-rich stretches of double-stranded DNA.[1] Isoform 2 binds to double-stranded DNA.[2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The hPar14 protein is a peptidyl prolyl cis/trans isomerase and is a human parvulin homologue. The hPar14 protein shows about 30 % sequence identity with the other human parvulin homologue, hPin1. Here, the solution structure of hPar14 was determined by nuclear magnetic resonance spectroscopy. The N-terminal 35 residues preceding the peptidyl prolyl isomerase domain of hPar14 are unstructured, whereas hPin1 possesses the WW domain at its N terminus. The fold of residues 36-131 of hPar14, which comprises a four-stranded beta-sheet and three alpha-helices, is superimposable onto that of the peptidyl prolyl isomerase domain of hPin1. To investigate the interaction of hPar14 with a substrate, the backbone chemical-shift changes of hPar14 were monitored during titration with a tetra peptide. Met90, Val91, and Phe94 around the N terminus of alpha3 showed large chemical-shift changes. These residues form a hydrophobic patch on the molecular surface of hPar14. Two of these residues are conserved and have been shown to interact with the proline residue of the substrate in hPin1. On the other hand, hPar14 lacks the hPin1 positively charged residues (Lys63, Arg68, and Arg69), which determine the substrate specificity of hPin1 by interacting with phosphorylated Ser or Thr preceding the substrate Pro, and exhibits a different structure in the corresponding region. Therefore, the mechanism determining the substrate specificity seems to be different between hPar14 and hPin1.
Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14.,Terada T, Shirouzu M, Fukumori Y, Fujimori F, Ito Y, Kigawa T, Yokoyama S, Uchida T J Mol Biol. 2001 Jan 26;305(4):917-26. PMID:11162102[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fujiyama-Nakamura S, Yoshikawa H, Homma K, Hayano T, Tsujimura-Takahashi T, Izumikawa K, Ishikawa H, Miyazawa N, Yanagida M, Miura Y, Shinkawa T, Yamauchi Y, Isobe T, Takahashi N. Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineage. Mol Cell Proteomics. 2009 Jul;8(7):1552-65. Epub 2009 Apr 14. PMID:19369196 doi:http://dx.doi.org/M900147-MCP200
- ↑ Fujiyama-Nakamura S, Yoshikawa H, Homma K, Hayano T, Tsujimura-Takahashi T, Izumikawa K, Ishikawa H, Miyazawa N, Yanagida M, Miura Y, Shinkawa T, Yamauchi Y, Isobe T, Takahashi N. Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineage. Mol Cell Proteomics. 2009 Jul;8(7):1552-65. Epub 2009 Apr 14. PMID:19369196 doi:http://dx.doi.org/M900147-MCP200
- ↑ Terada T, Shirouzu M, Fukumori Y, Fujimori F, Ito Y, Kigawa T, Yokoyama S, Uchida T. Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14. J Mol Biol. 2001 Jan 26;305(4):917-26. PMID:11162102 doi:http://dx.doi.org/10.1006/jmbi.2000.4293
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