2c3b: Difference between revisions
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THE CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS CYCLOPHILIN REVEALS 3D DOMAIN SWAPPING OF A CENTRAL ELEMENT
OverviewOverview
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.
About this StructureAbout this Structure
2C3B is a Single protein structure of sequence from Aspergillus fumigatus with SO4 as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of Aspergillus fumigatus cyclophilin reveals 3D domain swapping of a central element., Limacher A, Kloer DP, Fluckiger S, Folkers G, Crameri R, Scapozza L, Structure. 2006 Feb;14(2):185-95. PMID:16472738
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