1sp7: Difference between revisions
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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== | ||
<StructureSection load='1sp7' size='340' side='right' caption='[[1sp7]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='1sp7' size='340' side='right'caption='[[1sp7]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1sp7]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SP7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1sp7]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SP7 FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Collagen|Collagen]] | *[[Collagen 3D structures|Collagen 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Bachinger, H P]] | [[Category: Bachinger, H P]] | ||
[[Category: Grzesiek, S]] | [[Category: Grzesiek, S]] | ||
Revision as of 17:04, 18 December 2019
Structure of the Cys-rich C-terminal domain of Hydra minicollagenStructure of the Cys-rich C-terminal domain of Hydra minicollagen
Structural highlights
Publication Abstract from PubMedA 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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