4lav: Difference between revisions

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==Crystal Structure Analysis of FKBP52, Crystal Form II==
==Crystal Structure Analysis of FKBP52, Crystal Form II==
<StructureSection load='4lav' size='340' side='right' caption='[[4lav]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='4lav' size='340' side='right'caption='[[4lav]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4lav]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LAV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LAV FirstGlance]. <br>
<table><tr><td colspan='2'>[[4lav]] is a 2 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=4LAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LAV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q1c|1q1c]], [[4law|4law]], [[4lax|4lax]], [[4lay|4lay]]</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=4lav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lav OCA], [https://pdbe.org/4lav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lav RCSB], [https://www.ebi.ac.uk/pdbsum/4lav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lav ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP4, FKBP52 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4lav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lav OCA], [http://pdbe.org/4lav PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lav RCSB], [http://www.ebi.ac.uk/pdbsum/4lav PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lav ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/FKBP4_HUMAN FKBP4_HUMAN]] Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria.<ref>PMID:1279700</ref> <ref>PMID:1376003</ref> <ref>PMID:2378870</ref> <ref>PMID:19945390</ref> <ref>PMID:21730050</ref>
[https://www.uniprot.org/uniprot/FKBP4_HUMAN FKBP4_HUMAN] Immunophilin protein with PPIase and co-chaperone activities (By similarity). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments (By similarity). The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria.<ref>PMID:1279700</ref> <ref>PMID:1376003</ref> <ref>PMID:2378870</ref> <ref>PMID:19945390</ref> <ref>PMID:21730050</ref>  
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[FK506 binding protein|FK506 binding protein]]
*[[FKBP 3D structures|FKBP 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Large Structures]]
[[Category: Bracher, A]]
[[Category: Bracher A]]
[[Category: Haehle, A]]
[[Category: Haehle A]]
[[Category: Hausch, F]]
[[Category: Hausch F]]
[[Category: Kozany, C]]
[[Category: Kozany C]]
[[Category: Wild, P]]
[[Category: Wild P]]
[[Category: Zacharias, M]]
[[Category: Zacharias M]]
[[Category: Fk-506 binding domain]]
[[Category: Hsp90 cochaperone]]
[[Category: Immunophilin]]
[[Category: Isomerase]]
[[Category: Peptidyl-prolyl isomerase]]
[[Category: Protein folding]]