2utg
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="2utg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2utg, resolution 1.64Å" /> '''STRUCTURE AND REFINE...)
Next diff →
Revision as of 12:00, 21 November 2007
|
STRUCTURE AND REFINEMENT OF THE OXIDIZED P21 FORM OF UTEROGLOBIN AT 1.64 ANGSTROMS RESOLUTION
Overview
One of the monoclinic P21 forms of uteroglobin, a progesterone-binding, protein secreted by the rabbit uterus, was crystallized and subjected to, X-ray diffraction analysis at 1.64 A resolution. The analysis was refined, to an R factor of 0.19 and the 1096 non-hydrogen atomic positions are, known to an accuracy of about 0.18 A. The average isotropic temperature, factor B was 10.4 A2. Uteroglobin is a dimer of two independent, polypeptide chains of 70 residues linked by two disulfide bridges and, related by a pseudo binary axis. Each monomer is folded into four, alpha-helices. An oblong hydrophobic pocket is observed inside the dimer, and the possibility that it represents a progesterone-binding site is, discussed. The present model includes 165 possible sites for water, molecules, of which six are located in the hydrophobic pocket. Polar, groups are involved in hydrogen bonding (intramolecular, intermolecular or, with water molecules).
About this Structure
2UTG is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Structure and refinement of the oxidized P21 form of uteroglobin at 1.64 A resolution., Bally R, Delettre J, J Mol Biol. 1989 Mar 5;206(1):153-70. PMID:2704039
Page seeded by OCA on Wed Nov 21 14:07:33 2007
