1g5w
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= FABP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= FABP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1bwy|1BWY]], [[2hmb|2HMB]], [[1hmr|1HMR]], [[1hms|1HMS]], [[1hmt|1HMT]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5w OCA], [http://www.ebi.ac.uk/pdbsum/1g5w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g5w RCSB]</span> | ||
}} | }} | ||
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[[Category: selected-fit binding]] | [[Category: selected-fit binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:37:16 2008'' |
Revision as of 17:37, 30 March 2008
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| Gene: | FABP3 (Homo sapiens) | ||||||
| Related: | 1BWY, 2HMB, 1HMR, 1HMS, 1HMT
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATTY ACID BINDING PROTEIN
Overview
Recent advances in the characterization of fatty acid-binding proteins (FABPs) by NMR have enabled various research groups to investigate the function of these proteins in aqueous solution. The binding of fatty acid molecules to FABPs, which proceeds through a portal region on the protein surface, is of particular interest. In the present study we have determined the three-dimensional solution structure of human heart-type FABP by multi-dimensional heteronuclear NMR spectroscopy. Subsequently, in combination with data collected on a F57S mutant we have been able to show that different fatty acids induce distinct conformational states of the protein backbone in this portal region, depending on the chain length of the fatty acid ligand. This indicates that during the binding process the protein accommodates the ligand molecule by a "selected-fit" mechanism. In fact, this behaviour appears to be especially pronounced in the heart-type FABP, possibly due to a more rigid backbone structure compared with other FABPs, as suggested by recent NMR relaxation studies. Thus differences in the dynamic behaviours of these proteins may be the key to understanding the variations in ligand affinity and specificity within the FABP family.
About this Structure
1G5W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Spin-system heterogeneities indicate a selected-fit mechanism in fatty acid binding to heart-type fatty acid-binding protein (H-FABP)., Lucke C, Rademacher M, Zimmerman AW, van Moerkerk HT, Veerkamp JH, Ruterjans H, Biochem J. 2001 Mar 1;354(Pt 2):259-66. PMID:11171102
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