1m63 Summary

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Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes

The structure was published by Huai, Q., Kim, H.-Y., Liu, Y., et al., Mondragon, A., Liu, J.O., and Ke, H., in 2002 in a paper entitled "Crystal Structure of Calcineurin-Cyclophilin-Cyclosporin Shows Common But Distinct Recognition of Immunophilin-Drug Complexes" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 2002.

The experimental data on which the structure is based was also deposited.

This entry contains 20 copies of 4 unique biopolymers (complete list).

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms heterooctamers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A SERINE/THREONINE PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT, ALPHA ISOFORM Q08209 (1-372) (PP2BA_HUMAN)search Homo sapienssearch 100% 372 100%
E SERINE/THREONINE PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT, ALPHA ISOFORM Q08209 (1-372) (PP2BA_HUMAN)search Homo sapienssearch 100% 372 100%
B CALCINEURIN B SUBUNIT ISOFORM 1 P63098 (2-170) (CANB1_HUMAN)search Homo sapienssearch 91% 169 94%
F CALCINEURIN B SUBUNIT ISOFORM 1 P63098 (2-170) (CANB1_HUMAN)search Homo sapienssearch 91% 169 94%
C PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A P62937 (1-165) (PPIA_HUMAN)search Homo sapienssearch 99% 165 100%
G PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A P62937 (1-165) (PPIA_HUMAN)search Homo sapienssearch 99% 165 100%
D CYCLOSPORIN A Not available
TOLYPOCLADIUM INFLATUMsearch Not available 11 100%
H CYCLOSPORIN A Not available
TOLYPOCLADIUM INFLATUMsearch Not available 11 100%


This entry contains 3 unique UniProt proteins:

UniProt accession Name Organism PDB
Q08209 (1 - 372) SERINE/THREONINE PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT, ALPHA ISOFORM Homo sapiens
P63098 (2 - 170) CALCINEURIN B SUBUNIT ISOFORM 1 Homo sapiens
P62937 (1 - 165) PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, E (Q08209) Protein serine/threonine phosphatasesearch Purple Acid Phosphatase; chain A, domain 2search PF00149: Calcineurin-like phosphoesterasesearch
B, F (P63098) Calmodulin-likesearch EF-handsearch PF13202: EF handsearch, PF13499: EF-hand domain pairsearch
C, G (P62937) Cyclophilin (peptidylprolyl isomerase)search Cyclophilinsearch PF00160: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLDsearch
D, H

Chain Molecule NORINE reference
D, HCYCLOSPORIN ANOR00033

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A, E (Q08209) hydrolase activitysearch
B, F (P63098) calcium ion bindingsearch metal ion bindingsearch protein domain specific bindingsearch calmodulin bindingsearch protein bindingsearch calcium-dependent protein serine/threonine phosphatase activitysearch cytosolsearch plasma membranesearch nucleoplasmsearch cytoplasmsearch calcineurin complexsearch sarcolemmasearch membranesearch positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathwaysearch dephosphorylationsearch intrinsic apoptotic signaling pathwaysearch innate immune responsesearch apoptotic processsearch Fc-epsilon receptor signaling pathwaysearch
C, G (P62937) peptidyl-prolyl cis-trans isomerase activitysearch protein bindingsearch unfolded protein bindingsearch poly(A) RNA bindingsearch peptide bindingsearch virion bindingsearch isomerase activitysearch extracellular regionsearch cytosolsearch extracellular spacesearch nucleussearch cytoplasmsearch extracellular vesicular exosomesearch membranesearch protein foldingsearch positive regulation of viral genome replicationsearch viral processsearch platelet activationsearch entry into host cellsearch uncoating of virussearch lipid particle organizationsearch RNA-dependent DNA replicationsearch protein peptidyl-prolyl isomerizationsearch viral life cyclesearch platelet degranulationsearch establishment of integrated proviral latencysearch regulation of viral genome replicationsearch leukocyte migrationsearch blood coagulationsearch viral release from host cellsearch positive regulation of protein secretionsearch virion assemblysearch

Chain InterPro annotation
A, E Calcineurin-like phosphoesterase domain, apaH typesearch Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatasesearch Metallo-dependent phosphatase-likesearch
B, F EF-hand domainsearch EF-hand domain pairsearch EF-Hand 1, calcium-binding sitesearch
C, G Cyclophilin-type peptidyl-prolyl cis-trans isomerase domainsearch Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved sitesearch Cyclophilin-type peptidyl-prolyl cis-trans isomerasesearch Cyclophilin-like domainsearch
D, H