1t61

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1t61.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1t61.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1t61| PDB=1t61 | SCENE= }}
{{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===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15299013}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15299013 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15299013}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Nc1 domain]]
[[Category: Nc1 domain]]
[[Category: Type iv collagen]]
[[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 Mon Jul 28 15:34:07 2008''

Revision as of 12:34, 28 July 2008

Image:1t61.png

Template:STRUCTURE 1t61

crystal structure of collagen IV NC1 domain from placenta basement membrane

Template:ABSTRACT PUBMED 15299013

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 Mon Jul 28 15:34:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t61"
Personal tools