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The crystal structure of human cyclooxygenase-2 offers a unique opportunity for the design of new nonsteroidal anti-inflammatory drugs and may also provide insights into the mechanisms of membrane protein targeting and the role of prostaglandin physiology in inflammation and disease.
Two structures of bovine odorant binding protein show that this lipocalin is a domain-swapped dimer. The structures stimulate enticing ideas about how this protein transports such a large variety of odorant molecules to the olfactory receptors.
A new study demonstrates the use of enzymatic techniques of intermediate trapping and spectroscopic analysis in the protein crystal, and reports the structure of two specific catalytic intermediates formed during turnover by catalase.
The crystal structure of Plasmodium falciparum lactate dehydrogenase reveals a surprising shift in the position of the NADH cofactor that explains the unusual biochemical properties of this enzyme. There is also a distinctive surface cleft adjacent to the NADH binding pocket that forms an attractive target for inhibitor design.
NMR studies of the free and DNA-bound states of the lac represser headpiece show that formation of the hinge helix requires protein–protein interactions and occurs only when the represser binds to the full lac operator.
Rapid (millisecond) far-UV circular dichroism and fluorescence-monitored kinetic studies of the unfolding of barstar demonstrate the accumulation of a compact intermediate devoid of much secondary structure, before the rate limiting step in unfolding.
Two very fast phases in the incipient folding of apomyoglobin are assigned to the formation of the first local and global structural elements of the protein.
