1sp7

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{{STRUCTURE_1sp7| PDB=1sp7 | SCENE= }}
{{STRUCTURE_1sp7| PDB=1sp7 | SCENE= }}
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'''Structure of the Cys-rich C-terminal domain of Hydra minicollagen'''
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===Structure of the Cys-rich C-terminal domain of Hydra minicollagen===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15225618}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15225618 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15225618}}
==About this Structure==
==About this Structure==
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1SP7 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP7 OCA].
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1SP7 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP7 OCA].
==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15225618 15225618]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15225618 15225618]
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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]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bachinger, H P.]]
[[Category: Bachinger, H P.]]
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[[Category: Disulfide bond]]
[[Category: Disulfide bond]]
[[Category: Proline-rich]]
[[Category: Proline-rich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:58:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:30:18 2008''

Revision as of 21:30, 27 July 2008

Image:1sp7.png

Template:STRUCTURE 1sp7

Structure of the Cys-rich C-terminal domain of Hydra minicollagen

Template:ABSTRACT PUBMED 15225618

About this Structure

1SP7 is a Single protein structure. Full experimental information is available from OCA.

Reference

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

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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