User:Jan Panteli/sandbox 1
From Proteopedia
(Difference between revisions)
| Line 9: | Line 9: | ||
There are four domains to RBP, A,B,C,and D. These domains form a binding site for d-ribose and the bound form of the protein then interacts with transmembrane protein Trg, the chemotaxis transducer for d-ribose. | There are four domains to RBP, A,B,C,and D. These domains form a binding site for d-ribose and the bound form of the protein then interacts with transmembrane protein Trg, the chemotaxis transducer for d-ribose. | ||
| - | <Structure load='2dri' size='500' frame='true' align='right' caption='Closed conformation of the RBP upon binding with ligand, D-Ribose' scene='Insert optional scene name here' /> | + | <Structure load='2dri' size='500' frame='true' align='right' caption='Closed conformation of the RBP upon binding with ligand, D-Ribose in Domain A' scene='Insert optional scene name here' /> |
Revision as of 16:06, 4 May 2011
E. Coli D- Ribose Binding Protein (RBP) is involved in signal transduction of the chemokine D-ribose to stimulate chemotaxis in the bacteria.
One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
Exploring the Structure
|
There are four domains to RBP, A,B,C,and D. These domains form a binding site for d-ribose and the bound form of the protein then interacts with transmembrane protein Trg, the chemotaxis transducer for d-ribose.
|
