2c3b
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of Aspergillus fumigatus cyclophilin (Asp f 11) was | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Fluckiger, S.]] | [[Category: Fluckiger, S.]] | ||
[[Category: Folkers, G.]] | [[Category: Folkers, G.]] | ||
| - | [[Category: Kloer, D | + | [[Category: Kloer, D P.]] |
[[Category: Limacher, A.]] | [[Category: Limacher, A.]] | ||
[[Category: Scapozza, L.]] | [[Category: Scapozza, L.]] | ||
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[[Category: rotamase]] | [[Category: rotamase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:25 2008'' |
Revision as of 14:44, 21 February 2008
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THE CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS CYCLOPHILIN REVEALS 3D DOMAIN SWAPPING OF A CENTRAL ELEMENT
Overview
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 Structure
2C3B is a Single protein structure of sequence from Aspergillus fumigatus with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 16:44:25 2008
Categories: Aspergillus fumigatus | Single protein | Crameri, R. | Fluckiger, S. | Folkers, G. | Kloer, D P. | Limacher, A. | Scapozza, L. | SO4 | 3d domain swapping | Allergen | Asp f 11 | Isomerase | Misfolding | Ppiase | Rotamase
