1cwo: Difference between revisions
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|PDB= 1cwo |SIZE=350|CAPTION= <scene name='initialview01'>1cwo</scene>, resolution 1.86Å | |PDB= 1cwo |SIZE=350|CAPTION= <scene name='initialview01'>1cwo</scene>, resolution 1.86Å | ||
|SITE= <scene name='pdbsite=BIN:Cyclosporin+Binding+Site'>BIN</scene> | |SITE= <scene name='pdbsite=BIN:Cyclosporin+Binding+Site'>BIN</scene> | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene>, <scene name='pdbligand=VAD:DEAMINOHYDROXYVALINE'>VAD</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <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> | ||
|GENE= CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cwo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cwo OCA], [http://www.ebi.ac.uk/pdbsum/1cwo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cwo RCSB]</span> | |||
}} | }} | ||
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[[Category: complex (isomerase/immunosuppressant)]] | [[Category: complex (isomerase/immunosuppressant)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:30:05 2008'' | ||
Revision as of 19:30, 30 March 2008
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| , resolution 1.86Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , | ||||||
| Gene: | CYCLOPHILIN (Homo sapiens) | ||||||
| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN CYCLOPHILIN A COMPLEXED WITH THR2, LEU5, D-HIV8, LEU10 CYCLOSPORIN
OverviewOverview
The crystal structure of (Thr2, Leu5, d-Hiv8, Leu10)-cyclosporin (cyclic peptolide SDZ 214-103) has been determined as the unbound crystal form and as a complex with human cyclophilin A. This pair of structures provides an example of a significant difference in conformation between free and bound ligand in crystals. The conformation of the unbound form is unlike that of both free and bound conformations of cyclosporin A (with the amide bond between residues 3 and 4 in the cis conformation), while the bound conformation is similar to that of CsA bound to cyclophilin. The cyclophilin-bound conformations of both ligands are similar, though this involves a significantly different waterellipsisligand hydrogen-bonding structure, which compensates for the chemical differences between the two ligands.
About this StructureAbout this Structure
1CWO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Conformational differences of an immunosuppressant peptolide in a single crystal and in a crystal complex with human cyclophilin A., Mikol V, Taylor P, Kallen J, Walkinshaw MD, J Mol Biol. 1998 Oct 23;283(2):451-61. PMID:9769217
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