1gr3
From Proteopedia
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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. | ||
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| + | ==Disease== | ||
| + | Known diseases associated with this structure: Metaphyseal chondrodysplasia, Schmid type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120110 120110]], Spondylometaphyseal dysplasia, Japanese type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120110 120110]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: extracellular matrix]] | [[Category: extracellular matrix]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:08:09 2007'' |
Revision as of 15:01, 12 November 2007
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STRUCTURE OF THE HUMAN COLLAGEN X NC1 TRIMER
Contents |
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.
Disease
Known diseases associated with this structure: Metaphyseal chondrodysplasia, Schmid type OMIM:[120110], Spondylometaphyseal dysplasia, Japanese type OMIM:[120110]
About this Structure
1GR3 is a Single protein structure of sequence from Homo sapiens with CA, NA and CPS as ligands. Structure known Active Site: CPS. Full crystallographic information is available from OCA.
Reference
Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer., Bogin O, Kvansakul M, Rom E, Singer J, Yayon A, Hohenester E, Structure. 2002 Feb;10(2):165-73. PMID:11839302
Page seeded by OCA on Mon Nov 12 17:08:09 2007
Categories: Homo sapiens | Single protein | Bogin, O. | Hohenester, E. | Kvansakul, M. | Rom, E. | Singer, J. | Yayon, A. | CA | CPS | NA | Collagen | Connective tissue | Extracellular matrix
