2mph

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==Solution Structure of human FK506 binding Protein 25==
==Solution Structure of human FK506 binding Protein 25==
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<StructureSection load='2mph' size='340' side='right'caption='[[2mph]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2mph' size='340' side='right'caption='[[2mph]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2mph]] 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=2MPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MPH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2mph]] 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=2MPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MPH FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP3, FKBP25 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</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=2mph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mph OCA], [https://pdbe.org/2mph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mph RCSB], [https://www.ebi.ac.uk/pdbsum/2mph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mph ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
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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=2mph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mph OCA], [https://pdbe.org/2mph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mph RCSB], [https://www.ebi.ac.uk/pdbsum/2mph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mph ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/FKBP3_HUMAN FKBP3_HUMAN]] FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins.
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[https://www.uniprot.org/uniprot/FKBP3_HUMAN FKBP3_HUMAN] FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Human FKBP25, a nuclear protein, is a member of FK506 binding protein family (FKBP) and binds to immunosuppressive drugs such as FK506 and rapamycin. Human FKBP25 interacts with several nuclear proteins and regulates nuclear events. To understand the molecular basis of such interactions, we have performed NMR studies. Here, we report (1)H, (15)N and (13)C resonance assignments of the full-length human FKBP25 protein.
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The nuclear immunophilin FKBP25 interacts with chromatin-related proteins and transcription factors and is suggested to interact with nucleic acids. Currently the structural basis of nucleic acid binding by FKBP25 is unknown. Here we determined the nuclear magnetic resonance (NMR) solution structure of full-length human FKBP25 and studied its interaction with DNA. The FKBP25 structure revealed that the N-terminal helix-loop-helix (HLH) domain and C-terminal FK506-binding domain (FKBD) interact with each other and that both of the domains are involved in DNA binding. The HLH domain forms major-groove interactions and the basic FKBD loop cooperates to form interactions with an adjacent minor-groove of DNA. The FKBP25-DNA complex model, supported by NMR and mutational studies, provides structural and mechanistic insights into the nuclear immunophilin-mediated nucleic acid recognition.
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(1)H, (13)C and (15)N resonance assignments of human FK506 binding protein 25.,Prakash A, Shin J, Yoon HS Biomol NMR Assign. 2015 Apr;9(1):43-6. doi: 10.1007/s12104-014-9541-7. Epub 2014 , Jan 12. PMID:24414276<ref>PMID:24414276</ref>
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Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin.,Prakash A, Shin J, Rajan S, Yoon HS Nucleic Acids Res. 2016 Apr 7;44(6):2909-25. doi: 10.1093/nar/gkw001. Epub 2016, Jan 13. PMID:26762975<ref>PMID:26762975</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Prakash A]]
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[[Category: Prakash, A]]
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[[Category: Shin J]]
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[[Category: Shin, J]]
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[[Category: Yoon H]]
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[[Category: Yoon, H]]
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[[Category: Hfkbp25]]
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[[Category: Isomerase]]
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Revision as of 19:28, 19 October 2022

Solution Structure of human FK506 binding Protein 25

PDB ID 2mph

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