1H, 13C and 15N resonance assignments of Ca2+ bound collagen-binding domain derived from a clostridial collagenase.
(1)H, (15)N, and (13)C NMR assignments for 116 amino acids (Gly893-Lys1008) of a bacterial collagen-binding domain (CBD) derived from Clostridium histolyticum class I collagenase were accomplished. Clostridial collagenases hydrolyze insoluble collagen. One to three copies of collagen-binding domains (CBDs) are present at their C-termini, each of which is the minimal segment required for the binding to the insoluble substrate. CBD has been shown to be able to anchor fused growth factors for up to 10 days in vivo. Structural analysis of the small domain with the unique function provides insights into designing a novel drug delivery vehicle by the rational drug design.
Philominathan
Sagaya Theresa Leena
ST
Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, AR 72701, USA. pstleena@uark.edu
Matsushita
Osamu
O
Jordan
John Brad
JB
Sakon
Joshua
J
D000595:Amino Acid Sequence; D002118:Calcium / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D003094:Collagen / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D003012:Microbial Collagenase / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons
D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons; D003094:Collagen; D003012:Microbial Collagenase; D002118:Calcium