1gr3

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1gr3, resolution 2.00Å

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STRUCTURE OF THE HUMAN COLLAGEN X NC1 TRIMER

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.

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

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