1t61
From Proteopedia
(New page: 200px<br /><applet load="1t61" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t61, resolution 1.5Å" /> '''crystal structure of ...) |
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| - | [[Image:1t61.jpg|left|200px]]<br /><applet load="1t61" size=" | + | [[Image:1t61.jpg|left|200px]]<br /><applet load="1t61" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t61, resolution 1.5Å" /> | caption="1t61, resolution 1.5Å" /> | ||
'''crystal structure of collagen IV NC1 domain from placenta basement membrane'''<br /> | '''crystal structure of collagen IV NC1 domain from placenta basement membrane'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Collagen IV networks are present in all metazoa and underlie epithelia as | + | 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== | ==About this Structure== | ||
| - | 1T61 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with K, CL, CA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1T61 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T61 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bondar, O.]] | [[Category: Bondar, O.]] | ||
| - | [[Category: Friedman, D | + | [[Category: Friedman, D B.]] |
| - | [[Category: Hudson, B | + | [[Category: Hudson, B G.]] |
[[Category: Shanmugasundararaj, S.]] | [[Category: Shanmugasundararaj, S.]] | ||
[[Category: Sundaramoorthy, M.]] | [[Category: Sundaramoorthy, M.]] | ||
| - | [[Category: Vanacore, R | + | [[Category: Vanacore, R M.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: type iv collagen]] | [[Category: type iv collagen]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:16 2008'' |
Revision as of 13:10, 21 February 2008
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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
1T61 is a Protein complex structure of sequences from Bos taurus with , , and as ligands. 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 Thu Feb 21 15:10:16 2008
Categories: Bos taurus | Protein complex | Bondar, O. | Friedman, D B. | Hudson, B G. | Shanmugasundararaj, S. | Sundaramoorthy, M. | Vanacore, R M. | CA | CL | GOL | K | Basement membrane | Nc1 domain | Type iv collagen
