1sp7
From Proteopedia
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[[Image:1sp7.gif|left|200px]] | [[Image:1sp7.gif|left|200px]] | ||
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'''Structure of the Cys-rich C-terminal domain of Hydra minicollagen''' | '''Structure of the Cys-rich C-terminal domain of Hydra minicollagen''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SP7 is a [[Single protein]] structure | + | 1SP7 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Meier, S.]] | [[Category: Meier, S.]] | ||
[[Category: Pokidysheva, E.]] | [[Category: Pokidysheva, E.]] | ||
| - | [[Category: | + | [[Category: Cysteine-rich]] |
| - | [[Category: | + | [[Category: Disulfide bond]] |
| - | [[Category: | + | [[Category: Proline-rich]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:58:36 2008'' | |
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Revision as of 05:58, 3 May 2008
Structure of the Cys-rich C-terminal domain of Hydra minicollagen
Overview
A high-precision solution structure of the C-terminal minicollagen cysteine rich domain of Hydra has been determined using modern heteronuclear and weak alignment NMR techniques at natural isotope abundance. The domain consists of only 24 amino acids, six of which are prolines and six are cysteines bonded in disulfide bridges that constrain the structure into a new fold. The redox equilibrium of the structure has been characterized from a titration with glutathione. No local native structures are detectable in the reduced form. Thus, oxidation and folding are tightly coupled.
About this Structure
1SP7 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation., Meier S, Haussinger D, Pokidysheva E, Bachinger HP, Grzesiek S, FEBS Lett. 2004 Jul 2;569(1-3):112-6. PMID:15225618 Page seeded by OCA on Sat May 3 08:58:36 2008
