1nsg

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[[Image:1nsg.gif|left|200px]]
[[Image:1nsg.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1nsg |SIZE=350|CAPTION= <scene name='initialview01'>1nsg</scene>, resolution 2.2&Aring;
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The line below this paragraph, containing "STRUCTURE_1nsg", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=RAD:C49-METHYL+RAPAMYCIN'>RAD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= HUMAN HIPPOCAMPAL CDNA LIBRARY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_1nsg| PDB=1nsg | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nsg OCA], [http://www.ebi.ac.uk/pdbsum/1nsg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nsg RCSB]</span>
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}}
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'''THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP'''
'''THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP'''
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[[Category: Clardy, J.]]
[[Category: Clardy, J.]]
[[Category: Liang, J.]]
[[Category: Liang, J.]]
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[[Category: complex (isomerase/kinase)]]
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[[Category: Fkbp12]]
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[[Category: fkbp12]]
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[[Category: Frap]]
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[[Category: frap]]
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[[Category: Rapamycin]]
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[[Category: rapamycin]]
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[[Category: Transferase]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:55:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:34:51 2008''
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Revision as of 23:55, 2 May 2008

Template:STRUCTURE 1nsg

THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-RAPAMYCIN COMPLEX INTERACTING WITH HUMAN FRAP


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.

About this Structure

1NSG is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution., Liang J, Choi J, Clardy J, Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):736-44. PMID:10089303 Page seeded by OCA on Sat May 3 02:55:25 2008

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