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2utg

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{{STRUCTURE_2utg| PDB=2utg | SCENE= }}
{{STRUCTURE_2utg| PDB=2utg | SCENE= }}
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'''STRUCTURE AND REFINEMENT OF THE OXIDIZED P21 FORM OF UTEROGLOBIN AT 1.64 ANGSTROMS RESOLUTION'''
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===STRUCTURE AND REFINEMENT OF THE OXIDIZED P21 FORM OF UTEROGLOBIN AT 1.64 ANGSTROMS RESOLUTION===
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==Overview==
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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).
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{{ABSTRACT_PUBMED_2704039}}
==About this Structure==
==About this Structure==
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[[Category: Delettre, J.]]
[[Category: Delettre, J.]]
[[Category: Steroid binding]]
[[Category: Steroid binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:28:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:29:06 2008''

Revision as of 20:29, 27 July 2008

Image:2utg.png

Template:STRUCTURE 2utg

STRUCTURE AND REFINEMENT OF THE OXIDIZED P21 FORM OF UTEROGLOBIN AT 1.64 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 2704039

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 Sun Jul 27 23:29:06 2008

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