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1li1

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[[Image:1li1.gif|left|200px]]<br /><applet load="1li1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1li1.gif|left|200px]]
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caption="1li1, resolution 1.90&Aring;" />
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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'''<br />
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{{Structure
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|PDB= 1li1 |SIZE=350|CAPTION= <scene name='initialview01'>1li1</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene>
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|ACTIVITY=
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|GENE=
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}}
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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'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1LI1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LI1 OCA].
==Reference==
==Reference==
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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., 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12011424 12011424]
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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., 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:[http://www.ncbi.nlm.nih.gov/pubmed/12011424 12011424]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: protein-protein interaction]]
[[Category: protein-protein interaction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:31:06 2008''

Revision as of 10:31, 20 March 2008


PDB ID 1li1

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands:
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


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. 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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