1kth

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(New page: 200px<br /> <applet load="1kth" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kth, resolution 0.95&Aring;" /> '''The Anisotropic Ref...)
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Revision as of 15:48, 12 November 2007

Image:1kth.gif

1kth, resolution 0.95Å

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The Anisotropic Refinement Of Kunitz Type Domain C5 at 0.95 Angstrom

Contents

Overview

The C-terminal Kunitz-type domain from the alpha3 chain of human type VI, collagen (C5), a single amino-acid residue chain with three disulfide, bridges, was refined at 0.9 A resolution in a monoclinic form, space group, P2(1) with one molecule per asymmetric unit, using data collected at, cryogenic temperature (110 K). The average protein factor decreases from, 21 A(2) at room temperature (RT) to 12 A(2) at cryotemperature (100 K, CT). The spatially close N- and C-termini remain highly disordered. The, different structural motifs of C5 were analyzed in terms of rigid-body, displacement (TLS analyses) and show dominant libration motion for the, secondary structure.

Disease

Known diseases associated with this structure: Bethlem myopathy OMIM:[120250], Ullrich congenital muscular dystrophy OMIM:[120250]

About this Structure

1KTH is a Single protein structure of sequence from Homo sapiens with PO4 as ligand. Full crystallographic information is available from OCA.

Reference

Anisotropic behaviour of the C-terminal Kunitz-type domain of the alpha3 chain of human type VI collagen at atomic resolution (0.9 A)., Arnoux B, Ducruix A, Prange T, Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1252-4. Epub 2002, Jun 20. PMID:12077460

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