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| [[Image:1oog.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1oog| PDB=1oog | SCENE= }} | | {{STRUCTURE_1oog| PDB=1oog | SCENE= }} |
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| '''Complex of Drosophila odorant binding protein LUSH with propanol'''
| | ===Complex of Drosophila odorant binding protein LUSH with propanol=== |
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| ==Overview==
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| We have solved the high-resolution crystal structures of the Drosophila melanogaster alcohol-binding protein LUSH in complex with a series of short-chain n-alcohols. LUSH is the first known nonenzyme protein with a defined in vivo alcohol-binding function. The structure of LUSH reveals a set of molecular interactions that define a specific alcohol-binding site. A group of amino acids, Thr57, Ser52 and Thr48, form a network of concerted hydrogen bonds between the protein and the alcohol that provides a structural motif to increase alcohol-binding affinity at this site. This motif seems to be conserved in a number of mammalian ligand-gated ion channels that are directly implicated in the pharmacological effects of alcohol. Further, these sequences are found in regions of ion channels that are known to confer alcohol sensitivity. We suggest that the alcohol-binding site in LUSH represents a general model for alcohol-binding sites in proteins.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12881720}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12881720 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12881720}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lush]] | | [[Category: Lush]] |
| [[Category: Odorant binding]] | | [[Category: Odorant binding]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:06:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:06:01 2008'' |