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| - | [[Image:1fe3.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1fe3| PDB=1fe3 | SCENE= }} | | {{STRUCTURE_1fe3| PDB=1fe3 | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF HUMAN BRAIN FATTY ACID BINDING PROTEIN OLEIC ACID'''
| + | ===CRYSTAL STRUCTURE OF HUMAN BRAIN FATTY ACID BINDING PROTEIN OLEIC ACID=== |
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| - | ==Overview==
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| - | Expression of brain fatty acid-binding protein (B-FABP) is spatially and temporally correlated with neuronal differentiation during brain development. Isothermal titration calorimetry demonstrates that recombinant human B-FABP clearly exhibits high affinity for the polyunsaturated n-3 fatty acids alpha-linolenic acid, eicosapentaenoic acid, docosahexaenoic acid, and for monounsaturated n-9 oleic acid (K(d) from 28 to 53 nm) over polyunsaturated n-6 fatty acids, linoleic acid, and arachidonic acid (K(d) from 115 to 206 nm). B-FABP has low binding affinity for saturated long chain fatty acids. The three-dimensional structure of recombinant human B-FABP in complex with oleic acid shows that the oleic acid hydrocarbon tail assumes a "U-shaped" conformation, whereas in the complex with docosahexaenoic acid the hydrocarbon tail adopts a helical conformation. A comparison of the three-dimensional structures and binding properties of human B-FABP with other homologous FABPs, indicates that the binding specificity is in part the result of nonconserved amino acid Phe(104), which interacts with double bonds present in the lipid hydrocarbon tail. In this context, analysis of the primary and tertiary structures of human B-FABP provides a rationale for its high affinity and specificity for polyunsaturated fatty acids. The expression of B-FABP in glial cells and its high affinity for docosahexaenoic acid, which is known to be an important component of neuronal membranes, points toward a role for B-FABP in supplying brain abundant fatty acids to the developing neuron.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10854433}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10854433 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10854433}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lipid-binding protein]] | | [[Category: Lipid-binding protein]] |
| | [[Category: Oa]] | | [[Category: Oa]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:13:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:07:01 2008'' |
Revision as of 00:07, 1 July 2008
Template:STRUCTURE 1fe3
CRYSTAL STRUCTURE OF HUMAN BRAIN FATTY ACID BINDING PROTEIN OLEIC ACID
Template:ABSTRACT PUBMED 10854433
About this Structure
1FE3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure and thermodynamic analysis of human brain fatty acid-binding protein., Balendiran GK, Schnutgen F, Scapin G, Borchers T, Xhong N, Lim K, Godbout R, Spener F, Sacchettini JC, J Biol Chem. 2000 Sep 1;275(35):27045-54. PMID:10854433
Page seeded by OCA on Tue Jul 1 03:07:01 2008
