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New page: left|200px<br /><applet load="1ihg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ihg, resolution 1.80Å" /> '''Bovine Cyclophilin 4...
 
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[[Image:1ihg.gif|left|200px]]<br /><applet load="1ihg" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ihg, resolution 1.80&Aring;" />
'''Bovine Cyclophilin 40, monoclinic form'''<br />


==Overview==
==Bovine Cyclophilin 40, monoclinic form==
BACKGROUND: The "large immunophilin" family consists of domains of, cyclophilin or FK506 binding protein linked to a tetratricopeptide (TPR), domain. They are intimately associated with steroid receptor complexes and, bind to the C-terminal domain of Hsp90 via the TPR domain. The competitive, binding of specific large immunophilins and other TPR-Hsp90 proteins, provides a regulatory mechanism for Hsp90 chaperone activity. RESULTS: We, have solved the X-ray structures of monoclinic and tetragonal forms of, Cyp40. In the monoclinic form, the TPR domain consists of seven helices of, variable length incorporating three TPR motifs, which provide a convincing, binding surface for the Hsp90 C-terminal MEEVD sequence. The C-terminal, residues of Cyp40 protrude out beyond the body of the TPR domain to form a, charged helix-the putative calmodulin binding site. However, in the, tetragonal form, two of the TPR helices have straightened out to form one, extended helix, providing a dramatically different conformation of the, molecule. CONCLUSIONS: The X-ray structures are consistent with the role, of Cyclophilin 40 as a multifunctional signaling protein involved in a, variety of protein-protein interactions. The intermolecular helix-helix, interactions in the tetragonal form mimic the intramolecular interactions, found in the fully folded monoclinic form. These conserved intra- and, intermolecular TPR-TPR interactions are illustrative of a high-fidelity, recognition mechanism. The two structures also open up the possibility, that partially folded forms of TPR may be important in domain swapping and, protein recognition.
<StructureSection load='1ihg' size='340' side='right'caption='[[1ihg]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ihg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IHG 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=1ihg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ihg OCA], [https://pdbe.org/1ihg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ihg RCSB], [https://www.ebi.ac.uk/pdbsum/1ihg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ihg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PPID_BOVIN PPID_BOVIN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis.<ref>PMID:1544925</ref> <ref>PMID:16650407</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/ih/1ihg_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=1ihg ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1IHG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with GOL 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=1IHG OCA].
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
 
== References ==
==Reference==
<references/>
Two structures of cyclophilin 40: folding and fidelity in the TPR domains., Taylor P, Dornan J, Carrello A, Minchin RF, Ratajczak T, Walkinshaw MD, Structure. 2001 May 9;9(5):431-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11377203 11377203]
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Carrello A]]
[[Category: Carrello, A.]]
[[Category: Dornan J]]
[[Category: Dornan, J.]]
[[Category: Minchin RF]]
[[Category: Minchin, R.F.]]
[[Category: Ratajczak T]]
[[Category: Ratajczak, T.]]
[[Category: Taylor P]]
[[Category: Taylor, P.]]
[[Category: Walkinshaw MD]]
[[Category: Walkinshaw, M.D.]]
[[Category: GOL]]
[[Category: ppiase immunophilin tetratricopeptide]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:23:59 2007''

Latest revision as of 10:35, 7 February 2024

Bovine Cyclophilin 40, monoclinic formBovine Cyclophilin 40, monoclinic form

Structural highlights

1ihg is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PPID_BOVIN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Kieffer LJ, Thalhammer T, Handschumacher RE. Isolation and characterization of a 40-kDa cyclophilin-related protein. J Biol Chem. 1992 Mar 15;267(8):5503-7. PMID:1544925
  2. ↑ Mok D, Allan RK, Carrello A, Wangoo K, Walkinshaw MD, Ratajczak T. The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains. FEBS Lett. 2006 May 15;580(11):2761-8. Epub 2006 Apr 24. PMID:16650407 doi:http://dx.doi.org/10.1016/j.febslet.2006.04.039

1ihg, resolution 1.80Å

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