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- | [[Image:1li1.gif|left|200px]] | + | {{Seed}} |
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| {{STRUCTURE_1li1| PDB=1li1 | SCENE= }} | | {{STRUCTURE_1li1| PDB=1li1 | SCENE= }} |
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- | '''The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link'''
| + | ===The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link=== |
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- | ==Overview==
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- | Triple-helical collagen IV protomers associate through their N- and C-termini forming a three-dimensional network, which provides basement membranes with an anchoring scaffold and mechanical strength. The noncollagenous (NC1) domain of the C-terminal junction between two adjacent collagen IV protomers from human placenta was crystallized and its 1.9-A structure was solved by multiple anomalous diffraction (MAD) phasing. This hexameric NC1 particle is composed of two trimeric caps, which interact through a large planar interface. Each cap is formed by two alpha 1 fragments and one alpha 2 fragment with a similar previously uncharacterized fold, segmentally arranged around an axial tunnel. Each monomer chain folds into two structurally very similar subdomains, which each contain a finger-like hairpin loop that inserts into a six-stranded beta-sheet of the neighboring subdomain of the same or the adjacent chain. Thus each trimer forms a quite regular, but nonclassical, sixfold propeller. The trimer-trimer interaction is further stabilized by a previously uncharacterized type of covalent cross-link between the side chains of a Met and a Lys residue of the alpha 1 and alpha 2 chains from opposite trimers, explaining previous findings of nonreducible cross-links in NC1. This structure provides insights into NC1-related diseases such as Goodpasture and Alport syndromes.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12011424}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 12011424 is the PubMed ID number. |
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| + | {{ABSTRACT_PUBMED_12011424}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Nc1 domain]] | | [[Category: Nc1 domain]] |
| [[Category: Protein-protein interaction]] | | [[Category: Protein-protein interaction]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:56:25 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:57:11 2008'' |
Revision as of 17:57, 2 July 2008
Template:STRUCTURE 1li1
The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link
Template:ABSTRACT PUBMED 12011424
About this Structure
1LI1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link., Than ME, Henrich S, Huber R, Ries A, Mann K, Kuhn K, Timpl R, Bourenkov GP, Bartunik HD, Bode W, Proc Natl Acad Sci U S A. 2002 May 14;99(10):6607-12. PMID:12011424
Page seeded by OCA on Wed Jul 2 20:57:11 2008
Categories: Homo sapiens | Protein complex | Bartunik, H D. | Bode, W. | Bourenkov, G P. | Henrich, S. | Huber, R. | Kuhn, K. | Mann, K. | Ries, A. | Than, M E. | Timpl, R. | Basement membrane | Collagen iv | Covalent cross-link | Nc1 domain | Protein-protein interaction