1t61
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1t61.jpg|left|200px]] | [[Image:1t61.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1t61", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | | | + | {{STRUCTURE_1t61| PDB=1t61 | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''crystal structure of collagen IV NC1 domain from placenta basement membrane''' | '''crystal structure of collagen IV NC1 domain from placenta basement membrane''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T61 OCA]. | |
==Reference== | ==Reference== | ||
The alpha1.alpha2 network of collagen IV. Reinforced stabilization of the noncollagenous domain-1 by noncovalent forces and the absence of Met-Lys cross-links., Vanacore RM, Shanmugasundararaj S, Friedman DB, Bondar O, Hudson BG, Sundaramoorthy M, J Biol Chem. 2004 Oct 22;279(43):44723-30. Epub 2004 Aug 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299013 15299013] | The alpha1.alpha2 network of collagen IV. Reinforced stabilization of the noncollagenous domain-1 by noncovalent forces and the absence of Met-Lys cross-links., Vanacore RM, Shanmugasundararaj S, Friedman DB, Bondar O, Hudson BG, Sundaramoorthy M, J Biol Chem. 2004 Oct 22;279(43):44723-30. Epub 2004 Aug 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299013 15299013] | ||
| - | [[Category: Bos taurus]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Bondar, O.]] | [[Category: Bondar, O.]] | ||
[[Category: Friedman, D B.]] | [[Category: Friedman, D B.]] | ||
| Line 31: | Line 26: | ||
[[Category: Sundaramoorthy, M.]] | [[Category: Sundaramoorthy, M.]] | ||
[[Category: Vanacore, R M.]] | [[Category: Vanacore, R M.]] | ||
| - | [[Category: | + | [[Category: Basement membrane]] |
| - | [[Category: | + | [[Category: Nc1 domain]] |
| - | [[Category: | + | [[Category: Type iv collagen]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:34:21 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:34, 3 May 2008
crystal structure of collagen IV NC1 domain from placenta basement membrane
Overview
Collagen IV networks are present in all metazoa and underlie epithelia as a component of basement membranes. The networks are essential for tissue function and are defective in disease. They are assembled by the oligomerization of triple-helical protomers that are linked end-to-end. At the C terminus, two protomers are linked head-to-head by interactions of their trimeric noncollagenous domains, forming a hexamer structure. This linkage in the alpha1.alpha2 network is stabilized by a putative covalent Met-Lys cross-link between the trimer-trimer interface (Than, M. E., Henrich, S., Huber, R., Ries, A., Mann, K., Kuhn, K., Timpl, R., Bourenkov, G. P., Bartunik, H. D., and Bode, W. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 6607-6612) forming a nonreducible dimer that connects the hexamer. In the present study, this cross-link was further investigated by: (a) comparing the 1.5-A resolution crystal structures of the alpha1.alpha2 hexamers from bovine placenta and lens capsule basement membranes, (b) mass spectrometric analysis of monomer and nonreducible dimer subunits of placenta basement membrane hexamers, and (c) hexamer dissociation/re-association studies. The findings rule out the novel Met-Lys cross-link, as well as other covalent cross-links, but establish that the nonreducible dimer is an inherent structural feature of a subpopulation of hexamers. The dimers reflect the reinforced stabilization, by noncovalent forces, of the connection between two adjoining protomers of a network. The reinforcement extends to other types of collagen IV networks, and it underlies the cryptic nature of a B-cell epitope of the alpha3.alpha4.alpha5 hexamer, implicating the stabilization event in the etiology and pathogenesis of Goodpasture autoimmune disease.
About this Structure
Full crystallographic information is available from OCA.
Reference
The alpha1.alpha2 network of collagen IV. Reinforced stabilization of the noncollagenous domain-1 by noncovalent forces and the absence of Met-Lys cross-links., Vanacore RM, Shanmugasundararaj S, Friedman DB, Bondar O, Hudson BG, Sundaramoorthy M, J Biol Chem. 2004 Oct 22;279(43):44723-30. Epub 2004 Aug 5. PMID:15299013 Page seeded by OCA on Sat May 3 09:34:21 2008
