5MX0

Crystal structure of human fibromodulin

5MX0 の概要

• エントリーDOI: 10.2210/pdb5mx0/pdb
• 分子名称: Fibromodulin, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: leucine-rich repeat, extracellular matrix, collagen binding, structural protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix: Q06828
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87669.12

構造登録者

Paracuellos, P.,Hohenester, E. (登録日: 2017-01-20, 公開日: 2017-03-01, 最終更新日: 2024-11-13)

主引用文献

Paracuellos, P.,Kalamajski, S.,Bonna, A.,Bihan, D.,Farndale, R.W.,Hohenester, E.
Structural and functional analysis of two small leucine-rich repeat proteoglycans, fibromodulin and chondroadherin.
Matrix Biol., 63:106-116, 2017

PubMed Abstract: The small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assembly and cell signalling. We have determined crystal structures at ~2.2Å resolution of human fibromodulin and chondroadherin, two collagen-binding SLRPs. Their overall fold is similar to that of the prototypical SLRP, decorin, but unlike decorin neither fibromodulin nor chondroadherin forms a stable dimer. A previously identified binding site for integrin α2β1 maps to an α-helix in the C-terminal cap region of chondroadherin. Interrogation of the Collagen Toolkits revealed a unique binding site for chondroadherin in collagen II, and no binding to collagen III. A triple-helical peptide containing the sequence GAOGPSGFQGLOGPOGPO (O is hydroxyproline) forms a stable complex with chondroadherin in solution. In fibrillar collagen I and II, this sequence is aligned with the collagen cross-linking site KGHR, suggesting a role for chondroadherin in cross-linking.

PubMed: 28215822
DOI: 10.1016/j.matbio.2017.02.002

実験手法

X-RAY DIFFRACTION (2.21 Å)