Structural evidence for dimerization-regulated activation of an integral membrane phospolipase

Article Abstract:

It has been established that polar interactions can play a role in specific intermolecular contacts, even in the membrane-embedded parts of integral membrane proteins. Research in this area has involved investigating X-ray structures of monomeric and dimeric outer membrane phospholipase A from Escherichia coli. It was found that dimer interactions take place almost exclusively in the apolar membrane-embedded parts, with two hydrogen bonds within the hydrophobic membrane area being key interactions.

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Ion conduction pore is conserved among potassium channels

Article Abstract:

Research is presented describing the study of cell membrane flow conduction and the special function of potassium channels which allow K+ ions to pass through as membrane proteins.

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Maize yellow stripe1 encodes a membrane protein directly involve din Fe(III) uptake

Article Abstract:

It is demonstrated that yellow stripe1 is a membrane protein mediating iron uptake.

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