1XEC

Dimeric bovine tissue-extracted decorin, crystal form 2

1XEC の概要

• エントリーDOI: 10.2210/pdb1xec/pdb
• 関連するPDBエントリー: 1XCD 1XKU
• 分子名称: Decorin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: proteoglycan; leucine-rich repeat, structural protein
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix: P21793
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74279.94

構造登録者

Scott, P.G.,McEwan, P.A.,Dodd, C.M.,Bergmann, E.M.,Bishop, P.N.,Bella, J. (登録日: 2004-09-09, 公開日: 2004-11-02, 最終更新日: 2024-10-30)

主引用文献

Scott, P.G.,McEwan, P.A.,Dodd, C.M.,Bergmann, E.M.,Bishop, P.N.,Bella, J.
Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan
Proc.Natl.Acad.Sci.USA, 101:15633-15638, 2004

PubMed Abstract: Decorin is a ubiquitous extracellular matrix proteoglycan with a variety of important biological functions that are mediated by its interactions with extracellular matrix proteins, cytokines, and cell surface receptors. Decorin is the prototype of the family of small leucine-rich repeat proteoglycans and proteins (SLRPs), characterized by a protein core composed of leucine-rich repeats (LRRs), flanked by two cysteine-rich regions. We report here the crystal structure of the dimeric protein core of decorin, the best characterized member of the SLRP family. Each monomer adopts the curved solenoid fold characteristic of LRR domains, with a parallel beta-sheet on the inside interwoven with loops containing short segments of beta-strands, 3(10) helices, and polyproline II helices on the outside. Two main features are unique to this structure. First, decorin dimerizes through the concave surfaces of the LRR domains, which have been implicated previously in protein-ligand interactions. The amount of surface buried in this dimer rivals the buried surfaces of some of the highest-affinity macromolecular complexes reported to date. Second, the C-terminal region adopts an unusual capping motif that involves a laterally extended LRR and a disulfide bond. This motif seems to be unique to SLRPs and has not been observed in any other LRR protein structure to date. Possible implications of these features for decorin ligand binding and SLRP function are discussed.

PubMed: 15501918
DOI: 10.1073/pnas.0402976101

実験手法

X-RAY DIFFRACTION (2.3 Å)