STRUCTURE 1BM0
From Proteopedia
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==Abstract== | ==Abstract== | ||
| + | The three dimensional structures of pHSA and rHSA triclinic crystals were determined at 2.5A°resolution through multiple isomorphous replacement with a known tetragonal crystal. The pHSA and rHSA structures are similar with an r.m.s deviation of 0.24 A° for all the cα atoms. Cys 34 does not have a disulfide link with any ligand. A pocket of hydrophobic and positively charged residues is formed at domains 2 and 3 where a wide range of compounds can be accommodated. The surface of the domain has three binding sites for long chain fatty acids. | ||
Revision as of 00:09, 7 March 2010
Contents |
Abstract
The three dimensional structures of pHSA and rHSA triclinic crystals were determined at 2.5A°resolution through multiple isomorphous replacement with a known tetragonal crystal. The pHSA and rHSA structures are similar with an r.m.s deviation of 0.24 A° for all the cα atoms. Cys 34 does not have a disulfide link with any ligand. A pocket of hydrophobic and positively charged residues is formed at domains 2 and 3 where a wide range of compounds can be accommodated. The surface of the domain has three binding sites for long chain fatty acids.
Introduction
Crystallization of the tetragonal crystal
crystallization of the triclinic crystal
structural determination of the triclinic crystal
Results
Structural determination and quality
Local symmetry in the triclinic lattice
Overall structure
Subdomains
Free sulfhydryl group at cys34
Binding sites for drugs and other compounds
Conclusion
References
Proteopedia Page Contributors and Editors (what is this?)
Bhagiradhi Somalanka, Irene Becerra, Neeharika Pothuri, Michal Harel, Valerie Orovwigho
