2lhm: Difference between revisions

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[[Image:2lhm.jpg|left|200px]]
{{Seed}}
[[Image:2lhm.png|left|200px]]


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{{STRUCTURE_2lhm|  PDB=2lhm  |  SCENE=  }}  
{{STRUCTURE_2lhm|  PDB=2lhm  |  SCENE=  }}  


'''CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE'''
===CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE===




==Overview==
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The three-dimensional structures of apo- and holomutant human lysozymes (D86/92 lysozyme), in which a calcium binding site was designed and created for enhancing molecular stability by replacing both Gln86 and Ala92 with aspartic acids, were refined at 1.8-A resolution by x-ray crystallography. The overall structures and crystallographic thermal factors of all three proteins, the apo-, holo-D86/92, and the wild-type human lysozymes, were essentially identical; these results showed that the introduction of the calcium binding site did not affect either the overall structure or molecular rigidity of the proteins. However, structure analyses of the apo-D86/92 lysozyme revealed that the mutations affected the side chain conformation of residue 86 and hydrogen networks between the protein and the internal solvent molecules. In the structure of the holo-D86/92 lysozyme, seven oxygen ligands formed a slightly distorted pentagonal bipyramid around the calcium ion, indicating that the coordination around the calcium ion was quite similar to that in baboon alpha-lactalbumin. The pentagonal bipyramid coordination could be one of the most widely found and appropriate calcium binding schemes in proteins.
The line below this paragraph, {{ABSTRACT_PUBMED_1939116}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_1939116}}


==About this Structure==
==About this Structure==
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[[Category: Inaka, K.]]
[[Category: Inaka, K.]]
[[Category: Matsushima, M.]]
[[Category: Matsushima, M.]]
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