4msp: Difference between revisions
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==Disease== | ==Crystal structure of human peptidyl-prolyl cis-trans isomerase FKBP22 (aka FKBP14) containing two EF-hand motifs== | ||
<StructureSection load='4msp' size='340' side='right' caption='[[4msp]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4msp]] 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=4MSP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MSP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP14, FKBP22, UNQ322/PRO381 ([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=4msp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4msp OCA], [http://pdbe.org/4msp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4msp RCSB], [http://www.ebi.ac.uk/pdbsum/4msp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4msp ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/FKB14_HUMAN FKB14_HUMAN]] Ehlers-Danlos syndrome, kyphoscoliotic and deafness type. The disease is caused by mutations affecting the gene represented in this entry. | [[http://www.uniprot.org/uniprot/FKB14_HUMAN FKB14_HUMAN]] Ehlers-Danlos syndrome, kyphoscoliotic and deafness type. The disease is caused by mutations affecting the gene represented in this entry. | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/FKB14_HUMAN FKB14_HUMAN]] PPIases accelerate the folding of proteins during protein synthesis. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The FK506-binding protein (FKBP) family consists of proteins with a variety of protein-protein interaction domains and versatile cellular functions. It is assumed that all members are peptidyl-prolyl cis-trans isomerases with the enzymatic function attributed to the FKBP domain. Six members of this family localize to the mammalian endoplasmic reticulum (ER). Four of them, FKBP22 (encoded by the FKBP14 gene), FKBP23 (FKBP7), FKBP60 (FKBP9), and FKBP65 (FKBP10), are unique among all FKBPs as they contain the EF-hand motifs. Little is known about the biological roles of these proteins, but emerging genetics studies are attracting great interest to the ER resident FKBPs, as mutations in genes encoding FKBP10 and FKBP14 were shown to cause a variety of matrix disorders. Although the structural organization of the FKBP-type domain as well as of the EF-hand motif has been known for a while, it is difficult to conclude how these structures are combined and how it affects the protein functionality. We have determined a unique 1.9 A resolution crystal structure for human FKBP22, which can serve as a prototype for other EF hand-containing FKBPs. The EF-hand motifs of two FKBP22 molecules form a dimeric complex with an elongated and predominantly hydrophobic cavity that can potentially be occupied by an aliphatic ligand. The FKBP-type domains are separated by a cleft and their putative active sites can catalyze isomerazation of two bonds within a polypeptide chain in extended conformation. These structural results are of prime interest for understanding biological functions of ER resident FKBPs containing EF-hand motifs. | |||
Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs.,Boudko SP, Ishikawa Y, Nix J, Chapman MS, Bachinger HP Protein Sci. 2014 Jan;23(1):67-75. doi: 10.1002/pro.2391. Epub 2013 Nov 25. PMID:24272907<ref>PMID:24272907</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4msp" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[FK506 binding protein|FK506 binding protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human]] | |||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Bachinger, H P | [[Category: Bachinger, H P]] | ||
[[Category: Boudko, S P | [[Category: Boudko, S P]] | ||
[[Category: Ishikawa, Y | [[Category: Ishikawa, Y]] | ||
[[Category: Calcium binding]] | [[Category: Calcium binding]] | ||
[[Category: Ef-hand motif]] | [[Category: Ef-hand motif]] |
Revision as of 17:38, 4 August 2016
Crystal structure of human peptidyl-prolyl cis-trans isomerase FKBP22 (aka FKBP14) containing two EF-hand motifsCrystal structure of human peptidyl-prolyl cis-trans isomerase FKBP22 (aka FKBP14) containing two EF-hand motifs
Structural highlights
Disease[FKB14_HUMAN] Ehlers-Danlos syndrome, kyphoscoliotic and deafness type. The disease is caused by mutations affecting the gene represented in this entry. Function[FKB14_HUMAN] PPIases accelerate the folding of proteins during protein synthesis. Publication Abstract from PubMedThe FK506-binding protein (FKBP) family consists of proteins with a variety of protein-protein interaction domains and versatile cellular functions. It is assumed that all members are peptidyl-prolyl cis-trans isomerases with the enzymatic function attributed to the FKBP domain. Six members of this family localize to the mammalian endoplasmic reticulum (ER). Four of them, FKBP22 (encoded by the FKBP14 gene), FKBP23 (FKBP7), FKBP60 (FKBP9), and FKBP65 (FKBP10), are unique among all FKBPs as they contain the EF-hand motifs. Little is known about the biological roles of these proteins, but emerging genetics studies are attracting great interest to the ER resident FKBPs, as mutations in genes encoding FKBP10 and FKBP14 were shown to cause a variety of matrix disorders. Although the structural organization of the FKBP-type domain as well as of the EF-hand motif has been known for a while, it is difficult to conclude how these structures are combined and how it affects the protein functionality. We have determined a unique 1.9 A resolution crystal structure for human FKBP22, which can serve as a prototype for other EF hand-containing FKBPs. The EF-hand motifs of two FKBP22 molecules form a dimeric complex with an elongated and predominantly hydrophobic cavity that can potentially be occupied by an aliphatic ligand. The FKBP-type domains are separated by a cleft and their putative active sites can catalyze isomerazation of two bonds within a polypeptide chain in extended conformation. These structural results are of prime interest for understanding biological functions of ER resident FKBPs containing EF-hand motifs. Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs.,Boudko SP, Ishikawa Y, Nix J, Chapman MS, Bachinger HP Protein Sci. 2014 Jan;23(1):67-75. doi: 10.1002/pro.2391. Epub 2013 Nov 25. PMID:24272907[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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