2fap

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[[Image:2fap.gif|left|200px]]<br /><applet load="2fap" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fap.gif|left|200px]]
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caption="2fap, resolution 2.2&Aring;" />
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'''THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-(C16)-ETHOXY RAPAMYCIN COMPLEX INTERACTING WITH HUMA'''<br />
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{{Structure
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|PDB= 2fap |SIZE=350|CAPTION= <scene name='initialview01'>2fap</scene>, resolution 2.2&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=RAD:C49-METHYL RAPAMYCIN'>RAD</scene>
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|ACTIVITY= [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]
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|GENE= HUMAN HIPPOCAMPAL CDNA LIBRARY (CLONTECH, PALO ALTO, CA) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), 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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'''THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-(C16)-ETHOXY RAPAMYCIN COMPLEX INTERACTING WITH HUMA'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2FAP 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=RAD:'>RAD</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=2FAP OCA].
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2FAP is a [[Protein complex]] structure of sequences 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=2FAP OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10089303 10089303]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10089303 10089303]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
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[[Category: rapamycin]]
[[Category: rapamycin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:50:08 2008''

Revision as of 14:50, 20 March 2008


PDB ID 2fap

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands:
Gene: HUMAN HIPPOCAMPAL CDNA LIBRARY (CLONTECH, PALO ALTO, CA) (Homo sapiens), HUMAN HIPPOCAMPAL CDNA LIBRARY (Homo sapiens)
Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8
Coordinates: save as pdb, mmCIF, xml



THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-(C16)-ETHOXY RAPAMYCIN COMPLEX INTERACTING WITH HUMA


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

2FAP 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

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