1g5w
From Proteopedia
(New page: 200px<br /> <applet load="1g5w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g5w" /> '''SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATT...) |
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'''SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATTY ACID BINDING PROTEIN'''<br /> | '''SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATTY ACID BINDING PROTEIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G5W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1G5W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1G5W OCA]. |
==Reference== | ==Reference== | ||
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[[Category: selected-fit binding]] | [[Category: selected-fit binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:51:20 2008'' |
Revision as of 13:51, 15 February 2008
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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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