4fap: Difference between revisions

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[[Image:4fap.gif|left|200px]]<br />

[[Image:4fap.gif|left|200px]]<br /><applet load="4fap" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="4fap" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="4fap, resolution 2.80Å" />

'''ATOMIC STRUCTURES OF THE RAPAMYCIN ANALOGS IN COMPLEX WITH BOTH HUMAN FKBP12 AND FRB DOMAIN OF FRAP'''<br />

==Overview==

The structure of the FKBP12-rapamycin-FRB ternary complex has now been, refined at 2.2 A resolution. The cell-cycle arrest agent rapamycin binds, FK506-binding protein (FKBP12) and the FKBP12-rapamycin binding (FRB), domain of FKBP12-rapamycin associated protein (FRAP) simultaneously, and, the inhibition of FRAP is responsible for rapamycin's biological activity., The conformation of rapamycin in the ternary complex is very similar to, that observed in the FKBP12-rapamycin binary complex, with an r.m.s., difference of only 0.30 A. However, a slight (9 degrees ) rotation, repositions the FRB-binding face of rapamycin in the ternary complex., There are extensive rapamycin-protein interactions and relatively few, interactions between the two protein partners FKBP12 and FRB, these, interactions mainly involving residues in the 40s and 80s loops of FKBP12, and alpha1 and alpha4 of FRB. The high-resolution refinement has revealed, the crucial role of several buried waters in the formation of the ternary, complex.

The structure of the FKBP12-rapamycin-FRB ternary complex has now been refined at 2.2 A resolution. The cell-cycle arrest agent rapamycin binds FK506-binding protein (FKBP12) and the FKBP12-rapamycin binding (FRB) domain of FKBP12-rapamycin associated protein (FRAP) simultaneously, and the inhibition of FRAP is responsible for rapamycin's biological activity. The conformation of rapamycin in the ternary complex is very similar to that observed in the FKBP12-rapamycin binary complex, with an r.m.s. difference of only 0.30 A. However, a slight (9 degrees ) rotation repositions the FRB-binding face of rapamycin in the ternary complex. There are extensive rapamycin-protein interactions and relatively few interactions between the two protein partners FKBP12 and FRB, these interactions mainly involving residues in the 40s and 80s loops of FKBP12 and alpha1 and alpha4 of FRB. The high-resolution refinement has revealed the crucial role of several buried waters in the formation of the ternary complex.

==About this Structure==

4FAP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ARD as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=4FAP OCA].

4FAP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ARD:'>ARD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAP OCA].

==Reference==

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[[Category: rapamycin]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 23~~:50:~~29 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:15 2008''

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@@ Line 1: / Line 1: @@
-[[Image:4fap.gif|left|200px]]<br />
+[[Image:4fap.gif|left|200px]]<br /><applet load="4fap" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="4fap" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="4fap, resolution 2.80&Aring;" />
 '''ATOMIC STRUCTURES OF THE RAPAMYCIN ANALOGS IN COMPLEX WITH BOTH HUMAN FKBP12 AND FRB DOMAIN OF FRAP'''<br />
 ==Overview==
-The structure of the FKBP12-rapamycin-FRB ternary complex has now been, refined at 2.2 A resolution. The cell-cycle arrest agent rapamycin binds, FK506-binding protein (FKBP12) and the FKBP12-rapamycin binding (FRB), domain of FKBP12-rapamycin associated protein (FRAP) simultaneously, and, the inhibition of FRAP is responsible for rapamycin's biological activity., The conformation of rapamycin in the ternary complex is very similar to, that observed in the FKBP12-rapamycin binary complex, with an r.m.s., difference of only 0.30 A. However, a slight (9 degrees ) rotation, repositions the FRB-binding face of rapamycin in the ternary complex., There are extensive rapamycin-protein interactions and relatively few, interactions between the two protein partners FKBP12 and FRB, these, interactions mainly involving residues in the 40s and 80s loops of FKBP12, and alpha1 and alpha4 of FRB. The high-resolution refinement has revealed, the crucial role of several buried waters in the formation of the ternary, complex.
+The structure of the FKBP12-rapamycin-FRB ternary complex has now been refined at 2.2 A resolution. The cell-cycle arrest agent rapamycin binds FK506-binding protein (FKBP12) and the FKBP12-rapamycin binding (FRB) domain of FKBP12-rapamycin associated protein (FRAP) simultaneously, and the inhibition of FRAP is responsible for rapamycin's biological activity. The conformation of rapamycin in the ternary complex is very similar to that observed in the FKBP12-rapamycin binary complex, with an r.m.s. difference of only 0.30 A. However, a slight (9 degrees ) rotation repositions the FRB-binding face of rapamycin in the ternary complex. There are extensive rapamycin-protein interactions and relatively few interactions between the two protein partners FKBP12 and FRB, these interactions mainly involving residues in the 40s and 80s loops of FKBP12 and alpha1 and alpha4 of FRB. The high-resolution refinement has revealed the crucial role of several buried waters in the formation of the ternary complex.
 ==About this Structure==
-FAP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ARD as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4FAP OCA].
+FAP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ARD:'>ARD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FAP OCA].
 ==Reference==
@@ Line 24: / Line 23: @@
 [[Category: rapamycin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:50:29 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:15 2008''