1li1
From Proteopedia
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|PDB= 1li1 |SIZE=350|CAPTION= <scene name='initialview01'>1li1</scene>, resolution 1.90Å | |PDB= 1li1 |SIZE=350|CAPTION= <scene name='initialview01'>1li1</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1li1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1li1 OCA], [http://www.ebi.ac.uk/pdbsum/1li1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1li1 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | 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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Angiopathy, hereditary, with nephropathy, aneurysms, and muscle cramps OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120130 120130]], Brain small vessel disease with hemorrhage OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120130 120130]], Porencephaly OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120130 120130]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Than, M E.]] | [[Category: Than, M E.]] | ||
[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
| - | [[Category: ACT]] | ||
[[Category: basement membrane]] | [[Category: basement membrane]] | ||
[[Category: collagen iv]] | [[Category: collagen iv]] | ||
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[[Category: protein-protein interaction]] | [[Category: protein-protein interaction]] | ||
| - | ''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 22:03:05 2008'' |
Revision as of 19:03, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Overview
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.
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
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