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1cyn

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(New page: 200px<br /> <applet load="1cyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cyn, resolution 1.85&Aring;" /> '''CYCLOPHILIN B COMPL...)
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'''CYCLOPHILIN B COMPLEXED WITH [D-(CHOLINYLESTER)SER8]-CYCLOSPORIN'''<br />
'''CYCLOPHILIN B COMPLEXED WITH [D-(CHOLINYLESTER)SER8]-CYCLOSPORIN'''<br />
==Overview==
==Overview==
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The crystal structure of a complex between recombinant human cyclophilin B, (CypB) and a cyclosporin A (CsA) analog has been determined and refined at, 1.85-A resolution to a crystallographic R factor of 16.0%. The overall, structures of CypB and of cyclophilin A (CypA) are similar; however, significant differences occur in two loops and at the N and C termini. The, CsA-binding pocket in CypB has the same structure as in CypA and, cyclosporin shows a similar bound conformation and network of interactions, in both CypB and CypA complexes. The network of the water-mediated, contacts is also essentially conserved. The higher potency of the CypB/CsA, complex versus CypA/CsA in inhibiting the Ca(2+)- and calmodulin-dependent, protein phosphatase calcineurin is discussed in terms of the structural, differences between the two complexes. The three residues Arg90, Lys113, and Ala128 and the loop containing Arg158 on the surface of CypB are, likely to modulate the differences in calcineurin inhibition between CypA, and CypB.
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The crystal structure of a complex between recombinant human cyclophilin B (CypB) and a cyclosporin A (CsA) analog has been determined and refined at 1.85-A resolution to a crystallographic R factor of 16.0%. The overall structures of CypB and of cyclophilin A (CypA) are similar; however, significant differences occur in two loops and at the N and C termini. The CsA-binding pocket in CypB has the same structure as in CypA and cyclosporin shows a similar bound conformation and network of interactions in both CypB and CypA complexes. The network of the water-mediated contacts is also essentially conserved. The higher potency of the CypB/CsA complex versus CypA/CsA in inhibiting the Ca(2+)- and calmodulin-dependent protein phosphatase calcineurin is discussed in terms of the structural differences between the two complexes. The three residues Arg90, Lys113, and Ala128 and the loop containing Arg158 on the surface of CypB are likely to modulate the differences in calcineurin inhibition between CypA and CypB.
==About this Structure==
==About this Structure==
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1CYN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CYN OCA].
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1CYN is a [http://en.wikipedia.org/wiki/Single_protein 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=1CYN OCA].
==Reference==
==Reference==
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[[Category: Kallen, J.]]
[[Category: Kallen, J.]]
[[Category: Mikol, V.]]
[[Category: Mikol, V.]]
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[[Category: Walkinshaw, M.D.]]
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[[Category: Walkinshaw, M D.]]
[[Category: cyclosporin]]
[[Category: cyclosporin]]
[[Category: isomerase]]
[[Category: isomerase]]
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[[Category: signal]]
[[Category: signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:03 2008''

Revision as of 10:11, 21 February 2008

Image:1cyn.gif

1cyn, resolution 1.85Å

Drag the structure with the mouse to rotate

CYCLOPHILIN B COMPLEXED WITH [D-(CHOLINYLESTER)SER8]-CYCLOSPORIN

Overview

The crystal structure of a complex between recombinant human cyclophilin B (CypB) and a cyclosporin A (CsA) analog has been determined and refined at 1.85-A resolution to a crystallographic R factor of 16.0%. The overall structures of CypB and of cyclophilin A (CypA) are similar; however, significant differences occur in two loops and at the N and C termini. The CsA-binding pocket in CypB has the same structure as in CypA and cyclosporin shows a similar bound conformation and network of interactions in both CypB and CypA complexes. The network of the water-mediated contacts is also essentially conserved. The higher potency of the CypB/CsA complex versus CypA/CsA in inhibiting the Ca(2+)- and calmodulin-dependent protein phosphatase calcineurin is discussed in terms of the structural differences between the two complexes. The three residues Arg90, Lys113, and Ala128 and the loop containing Arg158 on the surface of CypB are likely to modulate the differences in calcineurin inhibition between CypA and CypB.

About this Structure

1CYN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A and delineation of its calcineurin-binding domain., Mikol V, Kallen J, Walkinshaw MD, Proc Natl Acad Sci U S A. 1994 May 24;91(11):5183-6. PMID:8197205

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