Title |
LRRML: a conformational database and an XML description of leucine-rich repeats (LRRs)
|
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Published in |
BMC Molecular and Cell Biology, November 2008
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DOI | 10.1186/1472-6807-8-47 |
Pubmed ID | |
Authors |
Tiandi Wei, Jing Gong, Ferdinand Jamitzky, Wolfgang M Heckl, Robert W Stark, Shaila C Rössle |
Abstract |
Leucine-rich repeats (LRRs) are present in more than 6000 proteins. They are found in organisms ranging from viruses to eukaryotes and play an important role in protein-ligand interactions. To date, more than one hundred crystal structures of LRR containing proteins have been determined. This knowledge has increased our ability to use the crystal structures as templates to model LRR proteins with unknown structures. Since the individual three-dimensional LRR structures are not directly available from the established databases and since there are only a few detailed annotations for them, a conformational LRR database useful for homology modeling of LRR proteins is desirable. |
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