2knt
From Proteopedia
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[[Image:2knt.gif|left|200px]] | [[Image:2knt.gif|left|200px]] | ||
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'''THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5''' | '''THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5''' | ||
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[[Category: Ducruix, A.]] | [[Category: Ducruix, A.]] | ||
[[Category: Merigeau, K.]] | [[Category: Merigeau, K.]] | ||
- | [[Category: | + | [[Category: Connective tissue]] |
- | [[Category: | + | [[Category: Extracellular matrix]] |
- | [[Category: | + | [[Category: Kunitz inhibitor]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:29:21 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 06:29, 4 May 2008
THE 1.2 ANGSTROM STRUCTURE OF KUNITZ TYPE DOMAIN C5
Overview
The recombinant Kunitz-type domain (C5) of human collagen alpha3(VI) chain was previously described at 1.6 A resolution at room temperature. By changing the crystallization conditions and using synchrotron radiation, we are able to record diffraction data to 1.2 A resolution for crystals of the same space group at 291 K. The protein-water-ion model has been refined anisotropically against these new data using the program SHELXL93; the results converged to an R factor of 15.0%, with all data between 7 and 1.2 A. The final electron-density map reveals a clear chain tracing with a few disordered residues and five residues out of 58 that present alternate conformations. The Cys14-Cys38 bond presents the less frequently observed left-hand conformation (chi1 = -60 degrees). The solvent molecules and a phosphate ion are well ordered with an average B of 38 A2. The high-resolution structure reveals the N and C termini which were missing from the 1.6 A structure.
About this Structure
2KNT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
1.2 A refinement of the Kunitz-type domain from the alpha3 chain of human type VI collagen., Merigeau K, Arnoux B, Perahia D, Norris K, Norris F, Ducruix A, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):306-12. PMID:9761897 Page seeded by OCA on Sun May 4 09:29:21 2008