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| - | [[Image:1sop.jpg|left|200px]] | |
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| - | <!--
| + | ==C-terminal cystine-rich domain of Minicollagen-I from Hydra== |
| - | The line below this paragraph, containing "STRUCTURE_1sop", creates the "Structure Box" on the page.
| + | <StructureSection load='1sop' size='340' side='right'caption='[[1sop]]' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[1sop]] 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=1SOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SOP FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> |
| - | {{STRUCTURE_1sop| PDB=1sop | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sop OCA], [https://pdbe.org/1sop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sop RCSB], [https://www.ebi.ac.uk/pdbsum/1sop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sop ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q00484_9CNID Q00484_9CNID] |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | The minicollagens found in the nematocysts of Hydra constitute a family of invertebrate collagens with unusual properties. They share a common modular architecture with a central collagen sequence ranging from 14 to 16 Gly-X-Y repeats flanked by polyproline/hydroxyproline stretches and short terminal domains that show a conserved cysteine pattern (CXXXCXXXCXXX-CXXXCC). The minicollagen cysteine-rich domains are believed to function in a switch of the disulfide connectivity from intra- to intermolecular bonds during maturation of the capsule wall. The solution structure of the C-terminal fragment including a minicollagen cysteine-rich domain of minicollagen-1 was determined in two independent groups by 1H NMR. The corresponding peptide comprising the last 24 residues of the molecule was produced synthetically and refolded by oxidation under low protein concentrations. Both presented structures are identical in their fold and disulfide connections (Cys2-Cys18, Cys6-Cys14, and Cys10-Cys19) revealing a robust structural motif that is supposed to serve as the polymerization module of the nematocyst capsule. |
| | | | |
| - | '''C-terminal cystine-rich domain of Minicollagen-I from Hydra'''
| + | The structure of the Cys-rich terminal domain of Hydra minicollagen, which is involved in disulfide networks of the nematocyst wall.,Pokidysheva E, Milbradt AG, Meier S, Renner C, Haussinger D, Bachinger HP, Moroder L, Grzesiek S, Holstein TW, Ozbek S, Engel J J Biol Chem. 2004 Jul 16;279(29):30395-401. Epub 2004 May 3. PMID:15123641<ref>PMID:15123641</ref> |
| - | | + | |
| - | | + | |
| - | ==Overview==
| + | |
| - | The minicollagens found in the nematocysts of Hydra constitute a family of invertebrate collagens with unusual properties. They share a common modular architecture with a central collagen sequence ranging from 14 to 16 Gly-X-Y repeats flanked by polyproline/hydroxyproline stretches and short terminal domains that show a conserved cysteine pattern (CXXXCXXXCXXX-CXXXCC). The minicollagen cysteine-rich domains are believed to function in a switch of the disulfide connectivity from intra- to intermolecular bonds during maturation of the capsule wall. The solution structure of the C-terminal fragment including a minicollagen cysteine-rich domain of minicollagen-1 was determined in two independent groups by 1H NMR. The corresponding peptide comprising the last 24 residues of the molecule was produced synthetically and refolded by oxidation under low protein concentrations. Both presented structures are identical in their fold and disulfide connections (Cys2-Cys18, Cys6-Cys14, and Cys10-Cys19) revealing a robust structural motif that is supposed to serve as the polymerization module of the nematocyst capsule.
| + | |
| | | | |
| - | ==About this Structure==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 1SOP is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOP OCA].
| + | </div> |
| | + | <div class="pdbe-citations 1sop" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Reference== | + | ==See Also== |
| - | The structure of the Cys-rich terminal domain of Hydra minicollagen, which is involved in disulfide networks of the nematocyst wall., Pokidysheva E, Milbradt AG, Meier S, Renner C, Haussinger D, Bachinger HP, Moroder L, Grzesiek S, Holstein TW, Ozbek S, Engel J, J Biol Chem. 2004 Jul 16;279(29):30395-401. Epub 2004 May 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15123641 15123641]
| + | *[[Collagen 3D structures|Collagen 3D structures]] |
| - | [[Category: Single protein]] | + | == References == |
| - | [[Category: Milbradt, A G.]] | + | <references/> |
| - | [[Category: Moroder, L.]] | + | __TOC__ |
| - | [[Category: Renner, C.]] | + | </StructureSection> |
| - | [[Category: Collagen oxidative refolding]] | + | [[Category: Hydra sp]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:57:38 2008''
| + | [[Category: Large Structures]] |
| | + | [[Category: Milbradt AG]] |
| | + | [[Category: Moroder L]] |
| | + | [[Category: Renner C]] |
| Structural highlights
Function
Q00484_9CNID
Publication Abstract from PubMed
The minicollagens found in the nematocysts of Hydra constitute a family of invertebrate collagens with unusual properties. They share a common modular architecture with a central collagen sequence ranging from 14 to 16 Gly-X-Y repeats flanked by polyproline/hydroxyproline stretches and short terminal domains that show a conserved cysteine pattern (CXXXCXXXCXXX-CXXXCC). The minicollagen cysteine-rich domains are believed to function in a switch of the disulfide connectivity from intra- to intermolecular bonds during maturation of the capsule wall. The solution structure of the C-terminal fragment including a minicollagen cysteine-rich domain of minicollagen-1 was determined in two independent groups by 1H NMR. The corresponding peptide comprising the last 24 residues of the molecule was produced synthetically and refolded by oxidation under low protein concentrations. Both presented structures are identical in their fold and disulfide connections (Cys2-Cys18, Cys6-Cys14, and Cys10-Cys19) revealing a robust structural motif that is supposed to serve as the polymerization module of the nematocyst capsule.
The structure of the Cys-rich terminal domain of Hydra minicollagen, which is involved in disulfide networks of the nematocyst wall.,Pokidysheva E, Milbradt AG, Meier S, Renner C, Haussinger D, Bachinger HP, Moroder L, Grzesiek S, Holstein TW, Ozbek S, Engel J J Biol Chem. 2004 Jul 16;279(29):30395-401. Epub 2004 May 3. PMID:15123641[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pokidysheva E, Milbradt AG, Meier S, Renner C, Haussinger D, Bachinger HP, Moroder L, Grzesiek S, Holstein TW, Ozbek S, Engel J. The structure of the Cys-rich terminal domain of Hydra minicollagen, which is involved in disulfide networks of the nematocyst wall. J Biol Chem. 2004 Jul 16;279(29):30395-401. Epub 2004 May 3. PMID:15123641 doi:10.1074/jbc.M403734200
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