1knt: Difference between revisions

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==Overview==

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.

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.

==Disease==

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[[Category: collagen type vi fragment]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==Disease==
@@ Line 28: / Line 28: @@
 [[Category: collagen type vi fragment]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:14:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:05 2008''