1KNT

THE 1.6 ANGSTROMS STRUCTURE OF THE KUNITZ-TYPE DOMAIN FROM THE ALPHA3 CHAIN OF THE HUMAN TYPE VI COLLAGEN

Summary for 1KNT

• Entry DOI: 10.2210/pdb1knt/pdb
• Descriptor: COLLAGEN TYPE VI, SULFATE ION (3 entities in total)
• Functional Keywords: collagen type vi fragment
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix (By similarity): P12111
• Total number of polymer chains: 1
• Total formula weight: 6735.57

Authors

Arnoux, B.,Merigeau, K.,Saludjian, P.,Norris, F.,Norris, K.,Bjorn, S.,Olsen, O.,Petersen, L.,Ducruix, A. (deposition date: 1994-08-18, release date: 1994-11-01, Last modification date: 2024-10-30)

Primary citation

Arnoux, B.,Merigeau, K.,Saludjian, P.,Norris, F.,Norris, K.,Bjorn, S.,Olsen, O.,Petersen, L.,Ducruix, A.
The 1.6 A structure of Kunitz-type domain from the alpha 3 chain of human type VI collagen.
J.Mol.Biol., 246:609-617, 1995

PubMed Abstract: The C-terminal Kunitz-type domain from the alpha 3 chain of human type VI collagen (C5), a single 58 amino acid residue chain with three disulfide bridges, was cloned, expressed and crystallized in a monoclonic form, space group P2(1), with a = 25.7 A, b = 38.2 A, c = 28.8 A and beta = 109 degrees. The structure was resolved by molecular replacement, using Alzheimer's protein precursor inhibitor and bovine pancreatic trypsin inhibitor three-dimensional structures as search models. The molecule with one sulfate ion and 43 associated water molecules was refined by XPLOR to an R-factor of 18.9% at 1.6 A. The molecule was not degraded by trypsin and did not inhibit trypsin or tested serine proteases. As opposed to the other Kunitz family members, C5 demonstrates left-handed chirality of the Cys14-Cys38 disulfide bond. Inversion of the Thr13 carbonyl and bulky side-chains at the interface with trypsin in a model of the C5-trypsin complex may explain the lack of inhibition of trypsin.

PubMed: 7533217
DOI: 10.1006/jmbi.1994.0112

Experimental method

X-RAY DIFFRACTION (1.6 Å)