1rot: Difference between revisions

Revision as of 17:55, 27 July 2008

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File:1rot.png

Template:STRUCTURE 1rot

STRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BINDING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURESTRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BINDING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE

Template:ABSTRACT PUBMED 8780506

About this StructureAbout this Structure

1ROT is a Single protein structure of sequence from Oryctolagus cuniculus. Full experimental information is available from OCA.

ReferenceReference

Three-dimensional structure of the immunophilin-like domain of FKBP59 in solution., Craescu CT, Rouviere N, Popescu A, Cerpolini E, Lebeau MC, Baulieu EE, Mispelter J, Biochemistry. 1996 Aug 27;35(34):11045-52. PMID:8780506

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

OCA

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-[[Image:1rot.gif|left|200px]]
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-'''STRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BINDING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE'''
+===STRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BINDING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE===
-==Overview==
+<!--
-FKBP59 is a protein usually associated with heat-shock protein hsp90 and steroid receptors. The N-terminal domain of the rabbit liver protein (149 amino acids) has a sequence homology with FKBP12, binds FK506 immunosuppressor, and has a peptidyl-prolyl cis-trans isomerase activity. The three-dimensional structure of this domain (FKBP59-I) was determined using homo- and heteronuclear multidimensional NMR spectroscopy, distance geometry, and molecular dynamics methods. Structure calculations used 1290 interproton distance restraints derived from nuclear Overhauser enhancement measurements, 29 dihedral phi angle restraints, and 92 hydrogen bond restraints. For the final 22 structures, the root mean square distance from the mean atomic coordinates, calculated for well-defined secondary structure fragments, is 0.47 +/- 0.05 and 1.26 +/- 0.15 A for backbone heavy atoms (N, C alpha, C') and for all non-hydrogen atoms, respectively. The global fold contains a twisted six-stranded antiparallel beta-sheet and a short alpha-helix packed on the hydrophobic side of the sheet. The 20 N-terminal and 12 C-terminal amino acids of the domain are disordered. The main-chain structure of FKBP59-I is globally similar to the NMR-derived and X-ray structures of unbound FKBP12. An unusual hydrogen bond interaction between the indole amino proton of Trp 89 and the aromatic cycle of Phe 129 was observed. This gives a large upfield shift (-4.8 ppm) and a significant exchange protection factor. The implications of the present structure determination on the ligand binding of FKBP59 are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_8780506}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8780506 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_8780506}}
 ==About this Structure==
-ROT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROT OCA].
+ROT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROT OCA].
 ==Reference==
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 [[Category: Fk506-binding protein]]
 [[Category: Peptidyl prolyl cis-trans isomerase]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:55:39 2008''