1fjd

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[[Image:1fjd.gif|left|200px]]
 
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{{Structure
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==HUMAN PARVULIN-LIKE PEPTIDYL PROLYL CIS/TRANS ISOMERASE, HPAR14==
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|PDB= 1fjd |SIZE=350|CAPTION= <scene name='initialview01'>1fjd</scene>
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<StructureSection load='1fjd' size='340' side='right'caption='[[1fjd]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE=
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<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>
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}}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/1fjd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''HUMAN PARVULIN-LIKE PEPTIDYL PROLYL CIS/TRANS ISOMERASE, HPAR14'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1fjd" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Fujimori, F.]]
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[[Category: Fujimori F]]
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[[Category: Fukumori, Y.]]
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[[Category: Fukumori Y]]
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[[Category: Ito, Y.]]
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[[Category: Ito Y]]
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[[Category: Kigawa, T.]]
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[[Category: Kigawa T]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Shirouzu M]]
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[[Category: Shirouzu, M.]]
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[[Category: Terada T]]
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[[Category: Terada, T.]]
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[[Category: Uchida T]]
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[[Category: Uchida, T.]]
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[[Category: Yokoyama S]]
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[[Category: Yokoyama, S.]]
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[[Category: parvulin]]
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[[Category: peptidyl prolyl cis/trans isomerase]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:09:52 2008''
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Current revision

HUMAN PARVULIN-LIKE PEPTIDYL PROLYL CIS/TRANS ISOMERASE, HPAR14

PDB ID 1fjd

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