1cwa: Difference between revisions

Revision as of 13:10, 21 February 2008

X-RAY STRUCTURE OF A MONOMERIC CYCLOPHILIN A-CYCLOSPORIN A CRYSTAL COMPLEX AT 2.1 ANGSTROMS RESOLUTION

OverviewOverview

The crystal structure of a complex between recombinant human cyclophilin A (Cyp) and cyclosporin A (CsA) has been determined from a novel orthorhombic crystal form that contains only one monomer of complex per asymmetric unit rather than five in the previously determined tetragonal structure. The structure has been refined at 2.1 A resolution to a crystallographic R-factor of 16.7%. The conformation of Cyp is practically unchanged with respect to the tetragonal form. A certain number of previously undefined side-chains have been located in the electron density and a very detailed picture of the ordered solvent structure has been obtained. The interactions between CsA and Cyp are conserved. A network of the possibly conserved, water-mediated contacts is described. The structure of CsA in the monomeric complex is similar to that of the decameric complex, but shows a few small differences in the so-called effector domain of CsA, probably due to differences in crystal environment. The fact that this monomeric crystal form can be obtained shows that the formation of pentamer or decamer complexes is not a generally observed phenomenon and is not a prerequisite for biological activity.

About this StructureAbout this Structure

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

ReferenceReference

X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution., Mikol V, Kallen J, Pflugl G, Walkinshaw MD, J Mol Biol. 1993 Dec 20;234(4):1119-30. PMID:8263916

Page seeded by OCA on Thu Feb 21 12:10:23 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1cwa.gif|left|200px]]<br /><applet load="1cwa" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cwa.gif|left|200px]]<br /><applet load="1cwa" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cwa, resolution 2.1&Aring;" />
 '''X-RAY STRUCTURE OF A MONOMERIC CYCLOPHILIN A-CYCLOSPORIN A CRYSTAL COMPLEX AT 2.1 ANGSTROMS RESOLUTION'''<br />
 ==Overview==
-The crystal structure of a complex between recombinant human cyclophilin A, (Cyp) and cyclosporin A (CsA) has been determined from a novel, orthorhombic crystal form that contains only one monomer of complex per, asymmetric unit rather than five in the previously determined tetragonal, structure. The structure has been refined at 2.1 A resolution to a, crystallographic R-factor of 16.7%. The conformation of Cyp is practically, unchanged with respect to the tetragonal form. A certain number of, previously undefined side-chains have been located in the electron density, and a very detailed picture of the ordered solvent structure has been, obtained. The interactions between CsA and Cyp are conserved. A network of, the possibly conserved, water-mediated contacts is described. The, structure of CsA in the monomeric complex is similar to that of the, decameric complex, but shows a few small differences in the so-called, effector domain of CsA, probably due to differences in crystal, environment. The fact that this monomeric crystal form can be obtained, shows that the formation of pentamer or decamer complexes is not a, generally observed phenomenon and is not a prerequisite for biological, activity.
+The crystal structure of a complex between recombinant human cyclophilin A (Cyp) and cyclosporin A (CsA) has been determined from a novel orthorhombic crystal form that contains only one monomer of complex per asymmetric unit rather than five in the previously determined tetragonal structure. The structure has been refined at 2.1 A resolution to a crystallographic R-factor of 16.7%. The conformation of Cyp is practically unchanged with respect to the tetragonal form. A certain number of previously undefined side-chains have been located in the electron density and a very detailed picture of the ordered solvent structure has been obtained. The interactions between CsA and Cyp are conserved. A network of the possibly conserved, water-mediated contacts is described. The structure of CsA in the monomeric complex is similar to that of the decameric complex, but shows a few small differences in the so-called effector domain of CsA, probably due to differences in crystal environment. The fact that this monomeric crystal form can be obtained shows that the formation of pentamer or decamer complexes is not a generally observed phenomenon and is not a prerequisite for biological activity.
 ==About this Structure==
-CWA 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=1CWA OCA].
+CWA 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=1CWA OCA].
 ==Reference==
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 [[Category: Kallen, J.]]
 [[Category: Mikol, V.]]
-[[Category: Walkinshaw, M.D.]]
+[[Category: Walkinshaw, M D.]]
 [[Category: complex (isomerase/immunosuppressant)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:48:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:23 2008''