1fkf: Difference between revisions

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[[Image:1fkf.gif|left|200px]]<br />

[[Image:1fkf.gif|left|200px]]<br /><applet load="1fkf" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1fkf" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1fkf, resolution 1.7Å" />

'''ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX'''<br />

==Overview==

The structure of the human FK506 binding protein (FKBP), complexed with, the immunosuppressant FK506, has been determined to 1.7 angstroms, resolution by x-ray crystallography. The conformation of the protein, changes little upon complexation, but the conformation of FK506 is, markedly different in the bound and unbound forms. The drug's association, with the protein involves five hydrogen bonds, a hydrophobic binding, pocket lined with conserved aromatic residues, and an unusual carbonyl, binding pocket. The nature of this complex has implications for the, mechanism of rotamase catalysis and for the biological actions of FK506, and rapamycin.

The structure of the human FK506 binding protein (FKBP), complexed with the immunosuppressant FK506, has been determined to 1.7 angstroms resolution by x-ray crystallography. The conformation of the protein changes little upon complexation, but the conformation of FK506 is markedly different in the bound and unbound forms. The drug's association with the protein involves five hydrogen bonds, a hydrophobic binding pocket lined with conserved aromatic residues, and an unusual carbonyl binding pocket. The nature of this complex has implications for the mechanism of rotamase catalysis and for the biological actions of FK506 and rapamycin.

==About this Structure==

1FKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with FK5 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1FKF OCA].

1FKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FK5:'>FK5</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FKF OCA].

==Reference==

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[[Category: Single protein]]

[[Category: Clardy, J.]]

[[Category: Karplus, P.A.]]

[[Category: Karplus, P A.]]

[[Category: Schreiber, S.L.]]

[[Category: Schreiber, S L.]]

[[Category: Standaert, R.F.]]

[[Category: Standaert, R F.]]

[[Category: Vanduyne, G.D.]]

[[Category: Vanduyne, G D.]]

[[Category: FK5]]

[[Category: isomerase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 16:54:~~08 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:37 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1fkf.gif|left|200px]]<br />
+[[Image:1fkf.gif|left|200px]]<br /><applet load="1fkf" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1fkf" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1fkf, resolution 1.7&Aring;" />
 '''ATOMIC STRUCTURE OF FKBP-FK506, AN IMMUNOPHILIN-IMMUNOSUPPRESSANT COMPLEX'''<br />
 ==Overview==
-The structure of the human FK506 binding protein (FKBP), complexed with, the immunosuppressant FK506, has been determined to 1.7 angstroms, resolution by x-ray crystallography. The conformation of the protein, changes little upon complexation, but the conformation of FK506 is, markedly different in the bound and unbound forms. The drug's association, with the protein involves five hydrogen bonds, a hydrophobic binding, pocket lined with conserved aromatic residues, and an unusual carbonyl, binding pocket. The nature of this complex has implications for the, mechanism of rotamase catalysis and for the biological actions of FK506, and rapamycin.
+The structure of the human FK506 binding protein (FKBP), complexed with the immunosuppressant FK506, has been determined to 1.7 angstroms resolution by x-ray crystallography. The conformation of the protein changes little upon complexation, but the conformation of FK506 is markedly different in the bound and unbound forms. The drug's association with the protein involves five hydrogen bonds, a hydrophobic binding pocket lined with conserved aromatic residues, and an unusual carbonyl binding pocket. The nature of this complex has implications for the mechanism of rotamase catalysis and for the biological actions of FK506 and rapamycin.
 ==About this Structure==
-FKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with FK5 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FKF OCA].
+FKF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FK5:'>FK5</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FKF OCA].
 ==Reference==
@@ Line 15: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Clardy, J.]]
-[[Category: Karplus, P.A.]]
+[[Category: Karplus, P A.]]
-[[Category: Schreiber, S.L.]]
+[[Category: Schreiber, S L.]]
-[[Category: Standaert, R.F.]]
+[[Category: Standaert, R F.]]
-[[Category: Vanduyne, G.D.]]
+[[Category: Vanduyne, G D.]]
 [[Category: FK5]]
 [[Category: isomerase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:54:08 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:37 2008''