Collagen-binding mode of vWF-A3 domain determined by a transferred cross-saturation experiment

2002 ◽  
Vol 10 (1) ◽  
pp. 53-58 ◽  
Author(s):  
Noritaka Nishida ◽  
Hiromi Sumikawa ◽  
Masayoshi Sakakura ◽  
Nobuhisa Shimba ◽  
Hideo Takahashi ◽  
...  
Keyword(s):  
Binding Mode ◽  
Collagen Binding ◽  
Saturation Experiment

scholarly journals Structural studies of the MMP-3 interaction with triple-helical collagen introduce new roles for the enzyme in tissue remodelling

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Szymon W. Manka ◽  
Dominique Bihan ◽  
Richard W. Farndale
Keyword(s):  
Binding Mode ◽  
Dependent Manner ◽  
Tissue Destruction ◽  
Tissue Remodelling ◽  
Collagen Binding ◽  
Matrix Metalloproteinase 3 ◽  
Interaction Sites ◽  
Binding Data ◽  
Collagen Iii ◽  
The Individual

AbstractMatrix metalloproteinase-3 (MMP-3) participates in normal extracellular matrix turnover during embryonic development, organ morphogenesis and wound healing, and in tissue-destruction associated with aneurysm, cancer, arthritis and heart failure. Despite its inability to cleave triple-helical collagens, MMP-3 can still bind to them, but the mechanism, location and role of binding are not known. We used the Collagen Toolkits, libraries of triple-helical peptides that embrace the entire helical domains of collagens II and III, to map MMP-3 interaction sites. The enzyme recognises five sites on collagen II and three sites on collagen III. They share a glycine-phenylalanine-hydroxyproline/alanine (GFO/A) motif that is recognised by the enzyme in a context-dependent manner. Neither MMP-3 zymogen (proMMP-3) nor the individual catalytic (Cat) and hemopexin (Hpx) domains of MMP-3 interact with the peptides, revealing cooperative binding of both domains to the triple helix. The Toolkit binding data combined with molecular modelling enabled us to deduce the putative collagen-binding mode of MMP-3, where all three collagen chains make contacts with the enzyme in the valley running across both Cat and Hpx domains. The observed binding pattern casts light on how MMP-3 could regulate collagen turnover and compete with various collagen-binding proteins regulating cell adhesion and proliferation.

scholarly journals Structural basis of the collagen-binding mode of discoidin domain receptor 2

2007 ◽  
Vol 26 (18) ◽  
pp. 4168-4176 ◽  
Author(s):  
Osamu Ichikawa ◽  
Masanori Osawa ◽  
Noritaka Nishida ◽  
Naoki Goshima ◽  
Nobuo Nomura ◽  
...  
Keyword(s):  
Binding Mode ◽  
Structural Basis ◽  
Collagen Binding ◽  
Discoidin Domain Receptor ◽  
Discoidin Domain Receptor 2

scholarly journals Structural studies of MMP-3 interaction with triple-helical collagen introduce the enzyme’s new roles in tissue remodelling

2019 ◽  
Author(s):  
Szymon W. Manka ◽  
Dominique Bihan ◽  
Richard W. Farndale
Keyword(s):  
Triple Helix ◽  
Binding Mode ◽  
Dependent Manner ◽  
Tissue Remodelling ◽  
Collagen Binding ◽  
Matrix Metalloproteinase 3 ◽  
Interaction Sites ◽  
Binding Data ◽  
Collagen Iii ◽  
The Individual

AbstractMatrix metalloproteinase-3 (MMP-3 or stromelysin 1) participates in normal extracellular matrix (ECM) turnover during embryonic development, organ morphogenesis and wound healing, and in tissue-destructive diseases, such as aneurysm, cancer, arthritis and heart failure. Despite its ability to hydrolyse numerous proteins in the ECM, MMP-3 fails to cleave the triple helix of interstitial fibrillar collagens. Nonetheless, it can still bind to these collagens although the mechanism, location and role of binding are not known. We used the Collagen Toolkits, libraries of triple-helical peptides that embrace the entire helical domains of collagens II and III, to map MMP-3 interaction sites. The enzyme recognises five sites on collagen II and three sites on collagen III. They share a glycine-phenylalanine-hydroxyproline/alanine (GFO/A) motif that is recognised by the enzyme in a context-dependent manner. Neither MMP-3 zymogen (proMMP-3) nor the individual catalytic (Cat) and hemopexin (Hpx) domains of MMP-3 interact with the peptides, revealing cooperative binding of both domains to the triple helix. The Toolkit binding data combined with molecular modelling enabled us to deduce the putative collagen-binding mode of MMP-3, where all three collagen chains make contacts with the enzyme in the valley running across both Cat and Hpx domains. The observed binding pattern casts light on how MMP-3 could regulate collagen turnover and compete with various collagen-binding proteins regulating cell adhesion and proliferation.

Keratinocyte growth factor binds to collagens of the gastrointestinal tract: Identification of the collagen binding structure

2001 ◽  
Vol 120 (5) ◽  
pp. A695-A695
Author(s):  
M RUEHL ◽  
I SCHOENFELDER ◽  
R FARNDALE ◽  
G KNIGHT ◽  
R SOMASUNDARAM ◽  
...  
Keyword(s):  
Gastrointestinal Tract ◽  
Growth Factor ◽  
Keratinocyte Growth Factor ◽  
Collagen Binding ◽  
Binding Structure

Experimental validation of the predicted TGR5 binding mode model

2015 ◽  
Vol 53 (01) ◽  
Author(s):  
L Spomer ◽  
CGW Gertzen ◽  
D Häussinger ◽  
H Gohlke ◽  
V Keitel
Keyword(s):  
Experimental Validation ◽  
Binding Mode

Plasma Derived von Willebrand Factor Preparations: Collagen Binding and Ristocetin Cofactor Activities

1997 ◽  
Vol 78 (02) ◽  
pp. 930-933 ◽  
Author(s):  
Ping Chang ◽  
D L Aronson
Keyword(s):  
Von Willebrand Factor ◽  
Functional Activity ◽  
Binding Activity ◽  
Collagen Binding ◽  
Binding Function ◽  
Cofactor Activity ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Ristocetin Cofactor ◽  
Ristocetin Cofactor Activity

SummaryFive plasma preparations (11 lots) used in the treatment of von Willebrand’s disease (vWD) were evaluated. The collagen binding function of von Willebrand factor (vWF) containing preparations was compared with the ristocetin cofactor activity and the vWF antigen. Some preparations have higher ratio of functional activity (ristocetin cofactor and collagen binding) relative to the antigen than is found in normal plasma. The ristocetin cofactor activity and the collagen binding activity are tightly correlated (r = .95). Ultracentrifugal (UCF) analysis was used to compare the size distribution of vWf antigen, ristocetin cofactor and collagen binding activity. The sedimentation of all of the vWF parameters in the plasma products was slower than in plasma. In plasma products the ristocetin cofactor activity sediments the most rapidly, the collagen binding activity is slower and the antigen the slowest. The collagen/antigen ratio decreases with decreasing vWF size. Assignment of potency to vWF containing preparations utilizing the collagen binding activity may be more precise and as accurate as with the traditional ristocetin cofactor assay.

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