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1li1
From Proteopedia
(New page: 200px<br /> <applet load="1li1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1li1, resolution 1.90Å" /> '''The 1.9-A crystal s...) |
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| - | [[Image:1li1.gif|left|200px]]<br /> | + | [[Image:1li1.gif|left|200px]]<br /><applet load="1li1" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1li1" size=" | + | |
caption="1li1, resolution 1.90Å" /> | caption="1li1, resolution 1.90Å" /> | ||
'''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'''<br /> | '''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'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Triple-helical collagen IV protomers associate through their N- and | + | 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== | ==Disease== | ||
| - | Known diseases associated with this structure: 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]] | + | 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== | ||
| - | 1LI1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LI1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LI1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Bartunik, H | + | [[Category: Bartunik, H D.]] |
[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
| - | [[Category: Bourenkov, G | + | [[Category: Bourenkov, G P.]] |
[[Category: Henrich, S.]] | [[Category: Henrich, S.]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
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[[Category: Mann, K.]] | [[Category: Mann, K.]] | ||
[[Category: Ries, A.]] | [[Category: Ries, A.]] | ||
| - | [[Category: Than, M | + | [[Category: Than, M E.]] |
[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
[[Category: ACT]] | [[Category: ACT]] | ||
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[[Category: protein-protein interaction]] | [[Category: protein-protein interaction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:08 2008'' |
Revision as of 11:45, 21 February 2008
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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
Contents |
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.
Disease
Known diseases associated with this structure: Angiopathy, hereditary, with nephropathy, aneurysms, and muscle cramps OMIM:[120130], Brain small vessel disease with hemorrhage OMIM:[120130], Porencephaly OMIM:[120130]
About this Structure
1LI1 is a Protein complex structure of sequences from Homo sapiens with as ligand. 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 Thu Feb 21 13:45:08 2008
