1cwo: Difference between revisions

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[[Image:1cwo.jpg|left|200px]]<br /><applet load="1cwo" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1cwo.jpg|left|200px]]
caption="1cwo, resolution 1.86&Aring;" />
 
'''HUMAN CYCLOPHILIN A COMPLEXED WITH THR2, LEU5, D-HIV8, LEU10 CYCLOSPORIN'''<br />
{{Structure
|PDB= 1cwo |SIZE=350|CAPTION= <scene name='initialview01'>1cwo</scene>, resolution 1.86&Aring;
|SITE= <scene name='pdbsite=BIN:Cyclosporin+Binding+Site'>BIN</scene>
|LIGAND=
|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]
|GENE= CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''HUMAN CYCLOPHILIN A COMPLEXED WITH THR2, LEU5, D-HIV8, LEU10 CYCLOSPORIN'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1CWO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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] Known structural/functional Site: <scene name='pdbsite=BIN:Cyclosporin+Binding+Site'>BIN</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CWO OCA].  
1CWO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CWO OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9769217 9769217]
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:[http://www.ncbi.nlm.nih.gov/pubmed/9769217 9769217]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
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[[Category: complex (isomerase/immunosuppressant)]]
[[Category: complex (isomerase/immunosuppressant)]]


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Revision as of 11:29, 20 March 2008

File:1cwo.jpg


PDB ID 1cwo

Drag the structure with the mouse to rotate
, resolution 1.86Å
Sites:
Gene: CYCLOPHILIN (Homo sapiens)
Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8
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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