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(Difference between revisions)
| Line 12: | Line 12: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Baubichon-Cortay, H]] |
[[Category: Chaptal, V]] | [[Category: Chaptal, V]] | ||
| - | [[Category: DiPietro, A]] | ||
[[Category: Falson, P]] | [[Category: Falson, P]] | ||
| - | [[Category: | + | [[Category: Gueguen-Chaignon, V]] |
[[Category: Magnard, S]] | [[Category: Magnard, S]] | ||
| + | [[Category: Pietro, A Di]] | ||
[[Category: Atp-binding cassette transporter]] | [[Category: Atp-binding cassette transporter]] | ||
[[Category: General-base mechanism]] | [[Category: General-base mechanism]] | ||
[[Category: Multidrug resistance protein 1]] | [[Category: Multidrug resistance protein 1]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 12:25, 18 March 2015
Nucleotide-free crystal structure of nucleotide-binding domain 1 from human MRP1 supports a general-base catalysis mechanism for ATP hydrolysis.
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