3ifb
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:3ifb.gif|left|200px]] | [[Image:3ifb.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_3ifb", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_3ifb| PDB=3ifb | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''NMR STUDY OF HUMAN INTESTINAL FATTY ACID BINDING PROTEIN''' | '''NMR STUDY OF HUMAN INTESTINAL FATTY ACID BINDING PROTEIN''' | ||
| Line 30: | Line 27: | ||
[[Category: Sacchettini, J C.]] | [[Category: Sacchettini, J C.]] | ||
[[Category: Zhang, F.]] | [[Category: Zhang, F.]] | ||
| - | [[Category: | + | [[Category: Fatty acid binding]] |
| - | [[Category: | + | [[Category: Fatty acid binding protein]] |
| - | [[Category: | + | [[Category: Intracellular lipid binding protein]] |
| - | [[Category: | + | [[Category: Single base polymorphism]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:04:37 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:04, 4 May 2008
NMR STUDY OF HUMAN INTESTINAL FATTY ACID BINDING PROTEIN
Overview
The human intestinal fatty acid binding protein (I-FABP) is a small (131 amino acids) protein which binds dietary long-chain fatty acids in the cytosol of enterocytes. Recently, an alanine to threonine substitution at position 54 in I-FABP has been identified which affects fatty acid binding and transport, and is associated with the development of insulin resistance in several populations including Mexican-Americans and Pima Indians. To investigate the molecular basis of the binding properties of I-FABP, the 3D solution structure of the more common form of human I-FABP (Ala54) was studied by multidimensional NMR spectroscopy. Recombinant I-FABP was expressed from E. coli in the presence and absence of 15N-enriched media. The sequential assignments for non-delipidated I-FABP were completed by using 2D homonuclear spectra (COSY, TOCSY and NOESY) and 3D heteronuclear spectra (NOESY-HMQC and TOCSY-HMQC). The tertiary structure of human I-FABP was calculated by using the distance geometry program DIANA based on 2519 distance constraints obtained from the NMR data. Subsequent energy minimization was carried out by using the program SYBYL in the presence of distance constraints. The conformation of human I-FABP consists of 10 antiparallel beta-strands which form two nearly orthogonal beta-sheets of five strands each, and two short alpha-helices that connect the beta-strands A and B. The interior of the protein consists of a water-filled cavity between the two beta-sheets. The NMR solution structure of human I-FABP is similar to the crystal structure of rat I-FABP. The NMR results show significant conformational variability of certain backbone segments around the postulated portal region for the entry and exit of fatty acid ligand.
About this Structure
3IFB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of human intestinal fatty acid binding protein: implications for ligand entry and exit., Zhang F, Lucke C, Baier LJ, Sacchettini JC, Hamilton JA, J Biomol NMR. 1997 Apr;9(3):213-28. PMID:9204553 Page seeded by OCA on Sun May 4 22:04:37 2008
