1fjd

<StructureSection load='1fjd' size='340' side='right'caption='[[1fjd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1fjd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>

</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>

[[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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== 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<ref>PMID:11162102</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1fjd" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Fujimori, F]]

[[Category: Fukumori, Y]]

[[Category: Ito, Y]]

[[Category: Kigawa, T]]

[[Category: Structural genomic]]

[[Category: Shirouzu, M]]

[[Category: Terada, T]]

[[Category: Uchida, T]]

[[Category: Yokoyama, S]]

[[Category: Rsgi]]