1b6c: Difference between revisions

New page: left|200px<br /> <applet load="1b6c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b6c, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF...
 
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1b6c.gif|left|200px]]<br />
<applet load="1b6c" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1b6c, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF-BETA RECEPTOR IN COMPLEX WITH FKBP12'''<br />


==Overview==
==CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF-BETA RECEPTOR IN COMPLEX WITH FKBP12==
Activation of the type I TGFbeta receptor (TbetaR-I) requires, phosphorylation of a regulatory segment known as the GS region, located, upstream of the serine/threonine kinase domain in the cytoplasmic portion, of the receptor. The crystal structure of a fragment of unphosphorylated, TbetaR-I, containing both the GS region and the catalytic domain, has been, determined in complex with the FK506-binding protein FKBP12. TbetaR-I, adopts an inactive conformation that is maintained by the unphosphorylated, GS region. FKBP12 binds to the GS region of the receptor, capping the, TbetaR-II phosphorylation sites and further stabilizing the inactive, conformation of TbetaR-I. Certain structural features at the catalytic, center of TbetaR-I are characteristic of tyrosine kinases rather than, Ser/Thr kinases.
<StructureSection load='1b6c' size='340' side='right'caption='[[1b6c]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1b6c]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B6C FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1b6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b6c OCA], [https://pdbe.org/1b6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b6c RCSB], [https://www.ebi.ac.uk/pdbsum/1b6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b6c 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/b6/1b6c_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=1b6c ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known diseases associated with this structure: Aortic aneurysm, familial thoracic 5 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190181 190181]], Furlong syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190181 190181]], Loeys-Dietz syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=190181 190181]]
*[[FKBP 3D structures|FKBP 3D structures]]
 
*[[TGF-beta receptor 3D structures|TGF-beta receptor 3D structures]]
==About this Structure==
== References ==
1B6C is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B6C OCA].
<references/>
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12., Huse M, Chen YG, Massague J, Kuriyan J, Cell. 1999 Feb 5;96(3):425-36. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10025408 10025408]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Chen Y-G]]
[[Category: Chen, Y.G.]]
[[Category: Huse M]]
[[Category: Huse, M.]]
[[Category: Kuriyan J]]
[[Category: Kuriyan, J.]]
[[Category: Massague J]]
[[Category: Massague, J.]]
[[Category: SO4]]
[[Category: complex (isomerase/protein kinase)]]
[[Category: receptor serine/threonine kinase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:06:31 2007''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA