1sop
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1sop |SIZE=350|CAPTION= <scene name='initialview01'>1sop</scene> | |PDB= 1sop |SIZE=350|CAPTION= <scene name='initialview01'>1sop</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sop OCA], [http://www.ebi.ac.uk/pdbsum/1sop PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sop RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Moroder, L.]] | [[Category: Moroder, L.]] | ||
[[Category: Renner, C.]] | [[Category: Renner, C.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: NH2]] | ||
[[Category: collagen oxidative refolding]] | [[Category: collagen oxidative refolding]] | ||
| - | ''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 23:44:59 2008'' |
Revision as of 20:45, 30 March 2008
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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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