1gr3: Difference between revisions
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|PDB= 1gr3 |SIZE=350|CAPTION= <scene name='initialview01'>1gr3</scene>, resolution 2.00Å | |PDB= 1gr3 |SIZE=350|CAPTION= <scene name='initialview01'>1gr3</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=CPS:Cps+Binding+Site+For+Chain+A'>CPS</scene> | |SITE= <scene name='pdbsite=CPS:Cps+Binding+Site+For+Chain+A'>CPS</scene> | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gr3 OCA], [http://www.ebi.ac.uk/pdbsum/1gr3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gr3 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
Collagen X is expressed specifically in the growth plate of long bones. Its C1q-like C-terminal NC1 domain forms a stable homotrimer and is crucial for collagen X assembly. Mutations in the NC1 domain cause Schmid metaphyseal chondrodysplasia (SMCD). The crystal structure at 2.0 A resolution of the human collagen X NC1 domain reveals an intimate trimeric assembly strengthened by a buried cluster of calcium ions. Three strips of exposed aromatic residues on the surface of NC1 trimer are likely to be involved in the supramolecular assembly of collagen X. Most internal SMCD mutations probably prevent protein folding, whereas mutations of surface residues may affect the collagen X suprastructure in a dominant-negative manner. | Collagen X is expressed specifically in the growth plate of long bones. Its C1q-like C-terminal NC1 domain forms a stable homotrimer and is crucial for collagen X assembly. Mutations in the NC1 domain cause Schmid metaphyseal chondrodysplasia (SMCD). The crystal structure at 2.0 A resolution of the human collagen X NC1 domain reveals an intimate trimeric assembly strengthened by a buried cluster of calcium ions. Three strips of exposed aromatic residues on the surface of NC1 trimer are likely to be involved in the supramolecular assembly of collagen X. Most internal SMCD mutations probably prevent protein folding, whereas mutations of surface residues may affect the collagen X suprastructure in a dominant-negative manner. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Singer, J.]] | [[Category: Singer, J.]] | ||
[[Category: Yayon, A.]] | [[Category: Yayon, A.]] | ||
[[Category: collagen]] | [[Category: collagen]] | ||
[[Category: connective tissue]] | [[Category: connective tissue]] | ||
[[Category: extracellular matrix]] | [[Category: extracellular matrix]] | ||
''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 20:49:39 2008'' | ||
