1sp7
From Proteopedia
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| - | [[Image:1sp7.gif|left|200px]] | ||
| - | + | ==Structure of the Cys-rich C-terminal domain of Hydra minicollagen== | |
| - | + | <StructureSection load='1sp7' size='340' side='right'caption='[[1sp7]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1sp7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydra_sp. Hydra sp.]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1SP7 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr> | |
| - | | | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sp7 OCA], [https://pdbe.org/1sp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sp7 RCSB], [https://www.ebi.ac.uk/pdbsum/1sp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sp7 ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/Q00484_9CNID Q00484_9CNID] | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
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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. | 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. | ||
| - | + | 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<ref>PMID:15225618</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1sp7" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Collagen 3D structures|Collagen 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Hydra sp]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bachinger HP]] | ||
| + | [[Category: Grzesiek S]] | ||
| + | [[Category: Haussinger D]] | ||
| + | [[Category: Meier S]] | ||
| + | [[Category: Pokidysheva E]] | ||
Current revision
Structure of the Cys-rich C-terminal domain of Hydra minicollagen
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