2mph
From Proteopedia
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| - | ''' | + | ==Solution Structure of human FK506 binding Protein 25== |
| + | <StructureSection load='2mph' size='340' side='right' caption='[[2mph]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mph]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MPH FirstGlance]. <br> | ||
| + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></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=2mph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mph OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mph RCSB], [http://www.ebi.ac.uk/pdbsum/2mph PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | (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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Prakash, A]] | [[Category: Prakash, A]] | ||
| + | [[Category: Shin, J]] | ||
[[Category: Yoon, H]] | [[Category: Yoon, H]] | ||
| - | [[Category: | + | [[Category: Hfkbp25]] |
| + | [[Category: Isomerase]] | ||
Revision as of 12:13, 20 May 2015
Solution Structure of human FK506 binding Protein 25
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