<p>A model of collagen docked to the Sgo0707 crystal structure using Firedock. A: The collagen triple helix is docked into the binding pocket of the N1-domain. B: Collagen is docked in the groove formed by the interface between the N1- and N2-domains.</p
Ab initio calculations of three models of collagen at positions Pro–Pro–Gly (1), Pro–Gly–Pro (2), an...
Fibrillar collagens are the most abundant proteins in the extracellular matrix. Not only do they pro...
ABSTRACT In this report, we present a hypothesis on the mechanism used by interstitial collagenases ...
AbstractWe have determined the crystal structure of a complex between the I domain of integrin α2β1 ...
Collagen plays several key roles in cell binding, tissue growth, and structural strengthening of the...
AbstractThe recently determined crystal structure of the complex between an integrin I domain and a ...
The crystal structure for the NC4 domain of collagen IX (NC4) has recently been reported (2uur). NC4...
<p>The non-helical, folded C-terminal end of the collagen molecule (top) extending from the triple-h...
Clostridium histolyticum secretes collagenases, ColG and ColH, that cause extensive tissue destructi...
The GFOGER motif in collagens (O denotes hydroxyproline) represents a high-affinity binding site for...
Integrins comprise of a large family of heterodimeric cell adhesion receptors consisting of an α- an...
Collagen IX is a heterotrimer of three alpha-chains, which consists of three COL domains (collagenou...
BODE W, REINEMER P, HUBER R, KLEINE T, SCHNIERER S, Tschesche H. THE X-RAY CRYSTAL-STRUCTURE OF THE ...
Type I collagen, the predominant protein of vertebrates, polymerizes with type III and V collagens a...
REINEMER P, GRAMS F, HUBER R, et al. STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N-TERMINUS IN THE S...
Ab initio calculations of three models of collagen at positions Pro–Pro–Gly (1), Pro–Gly–Pro (2), an...
Fibrillar collagens are the most abundant proteins in the extracellular matrix. Not only do they pro...
ABSTRACT In this report, we present a hypothesis on the mechanism used by interstitial collagenases ...
AbstractWe have determined the crystal structure of a complex between the I domain of integrin α2β1 ...
Collagen plays several key roles in cell binding, tissue growth, and structural strengthening of the...
AbstractThe recently determined crystal structure of the complex between an integrin I domain and a ...
The crystal structure for the NC4 domain of collagen IX (NC4) has recently been reported (2uur). NC4...
<p>The non-helical, folded C-terminal end of the collagen molecule (top) extending from the triple-h...
Clostridium histolyticum secretes collagenases, ColG and ColH, that cause extensive tissue destructi...
The GFOGER motif in collagens (O denotes hydroxyproline) represents a high-affinity binding site for...
Integrins comprise of a large family of heterodimeric cell adhesion receptors consisting of an α- an...
Collagen IX is a heterotrimer of three alpha-chains, which consists of three COL domains (collagenou...
BODE W, REINEMER P, HUBER R, KLEINE T, SCHNIERER S, Tschesche H. THE X-RAY CRYSTAL-STRUCTURE OF THE ...
Type I collagen, the predominant protein of vertebrates, polymerizes with type III and V collagens a...
REINEMER P, GRAMS F, HUBER R, et al. STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N-TERMINUS IN THE S...
Ab initio calculations of three models of collagen at positions Pro–Pro–Gly (1), Pro–Gly–Pro (2), an...
Fibrillar collagens are the most abundant proteins in the extracellular matrix. Not only do they pro...
ABSTRACT In this report, we present a hypothesis on the mechanism used by interstitial collagenases ...
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