5MX1

Crystal structure of human chondroadherin

Summary for 5MX1

• Entry DOI: 10.2210/pdb5mx1/pdb
• Descriptor: Chondroadherin, PHOSPHATE ION, NICKEL (II) ION, ... (5 entities in total)
• Functional Keywords: leucine-rich repeat, extracellular matrix, collagen binding, cell adhesion
• Biological source: Homo sapiens (Human)
• Cellular location: Secreted, extracellular space, extracellular matrix : O15335
• Total number of polymer chains: 2
• Total formula weight: 77920.71

Authors

Paracuellos, P.,Hohenester, E. (deposition date: 2017-01-20, release date: 2017-03-01, Last modification date: 2024-01-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.17 Å)