1fkt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:13, 27 March 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1fkt.gif|left|200px]]
 
-
{{Structure
+
==SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN==
-
|PDB= 1fkt |SIZE=350|CAPTION= <scene name='initialview01'>1fkt</scene>
+
<StructureSection load='1fkt' size='340' side='right'caption='[[1fkt]]' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<table><tr><td colspan='2'>[[1fkt]] 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=1FKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FKT FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
|GENE=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fkt OCA], [https://pdbe.org/1fkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fkt RCSB], [https://www.ebi.ac.uk/pdbsum/1fkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fkt ProSAT]</span></td></tr>
-
}}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FKB1A_HUMAN FKB1A_HUMAN] Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.<ref>PMID:9233797</ref> <ref>PMID:16720724</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/fk/1fkt_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=1fkt ConSurf].
 +
<div style="clear:both"></div>
-
'''SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN'''
+
==See Also==
-
 
+
*[[FKBP 3D structures|FKBP 3D structures]]
-
 
+
== References ==
-
==Overview==
+
<references/>
-
Immunophilins, when complexed to immunosuppressive ligands, appear to inhibit signal transduction pathways that result in exocytosis and transcription. The solution structure of one of these, the human FK506 and rapamycin binding protein (FKBP), has been determined by nuclear magnetic resonance (NMR). FKBP has a previously unobserved antiparallel beta-sheet folding topology that results in a novel loop crossing and produces a large cavity lined by a conserved array of aromatic residues; this cavity serves as the rotamase active site and drug-binding pocket. There are other significant structural features (such as a protruding positively charged loop and an apparently flexible loop) that may be involved in the biological activity of FKBP.
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1FKT 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=1FKT OCA].
+
-
 
+
-
==Reference==
+
-
Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin., Michnick SW, Rosen MK, Wandless TJ, Karplus M, Schreiber SL, Science. 1991 May 10;252(5007):836-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1709301 1709301]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Karplus, M.]]
+
[[Category: Karplus M]]
-
[[Category: Michnick, S W.]]
+
[[Category: Michnick SW]]
-
[[Category: Rosen, M K.]]
+
[[Category: Rosen MK]]
-
[[Category: Schreiber, S L.]]
+
[[Category: Schreiber SL]]
-
[[Category: Wandless, T J.]]
+
[[Category: Wandless TJ]]
-
[[Category: cis-trans isomerase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:10:25 2008''
+

Current revision

SOLUTION STRUCTURE OF FKBP, A ROTAMASE ENZYME AND RECEPTOR FOR FK506 AND RAPAMYCIN

PDB ID 1fkt

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fkt"
Personal tools