1sp7: Difference between revisions
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sp7 OCA], [http://www.ebi.ac.uk/pdbsum/1sp7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sp7 RCSB]</span> | |||
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:45:08 2008'' | ||
Revision as of 23:45, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the Cys-rich C-terminal domain of Hydra minicollagen
OverviewOverview
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 StructureAbout this Structure
1SP7 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
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
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