1knt
From Proteopedia
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|PDB= 1knt |SIZE=350|CAPTION= <scene name='initialview01'>1knt</scene>, resolution 1.6Å | |PDB= 1knt |SIZE=350|CAPTION= <scene name='initialview01'>1knt</scene>, resolution 1.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1knt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1knt OCA], [http://www.ebi.ac.uk/pdbsum/1knt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1knt RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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== | ||
| - | Known diseases associated with this structure: Bethlem myopathy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120250 120250]], Ullrich congenital muscular dystrophy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=120250 120250]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Petersen, L.]] | [[Category: Petersen, L.]] | ||
[[Category: Saludjian, P.]] | [[Category: Saludjian, P.]] | ||
| - | [[Category: SO4]] | ||
[[Category: collagen type vi fragment]] | [[Category: collagen type vi fragment]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:06 2008'' |
Revision as of 18:51, 30 March 2008
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| , resolution 1.6Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE 1.6 ANGSTROMS STRUCTURE OF THE KUNITZ-TYPE DOMAIN FROM THE ALPHA3 CHAIN OF THE HUMAN TYPE VI COLLAGEN
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.
About this Structure
1KNT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The 1.6 A structure of Kunitz-type domain from the alpha 3 chain of human type VI collagen., Arnoux B, Merigeau K, Saludjian P, Norris F, Norris K, Bjorn S, Olsen O, Petersen L, Ducruix A, J Mol Biol. 1995 Mar 10;246(5):609-17. PMID:7533217
Page seeded by OCA on Sun Mar 30 21:51:06 2008
