2c3b: Difference between revisions

The crystal structure of Aspergillus fumigatus cyclophilin (Asp f 11) was, solved by the multiwavelength anomalous dispersion method and was refined, to a resolution of 1.85 A with R and R(free) values of 18.9% and 21.4%, respectively. Many cyclophilin structures have been solved to date, all, showing the same monomeric conformation. In contrast, the structure of A., fumigatus cyclophilin reveals dimerization by 3D domain swapping and, represents one of the first proteins with a swapped central domain. The, domain-swapped element consists of two beta strands and a subsequent loop, carrying a conserved tryptophan. The tryptophan binds into the active, site, inactivating cis-trans isomerization. This might be a means of, biological regulation. The two hinge loops leave the protein prone to, misfolding. In this context, alternative forms of 3D domain swapping that, can lead to N- or C-terminally swapped dimers, oligomers, and aggregates, are discussed.

2C3B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C3B OCA].  

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