1sop
From Proteopedia
(New page: 200px<br /><applet load="1sop" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sop" /> '''C-terminal cystine-rich domain of Minicollag...) |
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| - | [[Image:1sop.jpg|left|200px]]<br /><applet load="1sop" size=" | + | [[Image:1sop.jpg|left|200px]]<br /><applet load="1sop" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''C-terminal cystine-rich domain of Minicollagen-I from Hydra'''<br /> | '''C-terminal cystine-rich domain of Minicollagen-I from Hydra'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The minicollagens found in the nematocysts of Hydra constitute a family of | + | 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== | ==About this Structure== | ||
| - | 1SOP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1SOP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SOP OCA]. |
==Reference== | ==Reference== | ||
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15123641 15123641] | 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15123641 15123641] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Milbradt, A | + | [[Category: Milbradt, A G.]] |
[[Category: Moroder, L.]] | [[Category: Moroder, L.]] | ||
[[Category: Renner, C.]] | [[Category: Renner, C.]] | ||
| Line 19: | Line 19: | ||
[[Category: collagen oxidative refolding]] | [[Category: collagen oxidative refolding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:03:39 2008'' |
Revision as of 13:03, 21 February 2008
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C-terminal cystine-rich domain of Minicollagen-I from Hydra
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
1SOP is a Single protein structure of sequence from [1] with and as ligands. Full crystallographic information is available from OCA.
Reference
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
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