1knt: Difference between revisions
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'''THE 1.6 ANGSTROMS STRUCTURE OF THE KUNITZ-TYPE DOMAIN FROM THE ALPHA3 CHAIN OF THE HUMAN TYPE VI COLLAGEN''' | {{Structure | ||
|PDB= 1knt |SIZE=350|CAPTION= <scene name='initialview01'>1knt</scene>, resolution 1.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THE 1.6 ANGSTROMS STRUCTURE OF THE KUNITZ-TYPE DOMAIN FROM THE ALPHA3 CHAIN OF THE HUMAN TYPE VI COLLAGEN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KNT is a [ | 1KNT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KNT OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7533217 7533217] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: collagen type vi fragment]] | [[Category: collagen type vi fragment]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:19:52 2008'' | ||
Revision as of 10:19, 20 March 2008
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| 1knt, resolution 1.6Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| 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.
Disease
Known diseases associated with this structure: Bethlem myopathy OMIM:[120250], Ullrich congenital muscular dystrophy OMIM:[120250]
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
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