
AbstractExtensive in silico search of the genome of Caenorhabditis elegans revealed the presence of 33 genes coding for globins that are all transcribed. These globins are very diverse in gene and protein structure and are localized in a variety of cells, mostly neurons. The large number of C. elegans globin genes is assumed to be the result of multiple evolutionary duplication and radiation events. Processes of subfunctionalization and diversification probably led to their cell‐specific expression patterns and fixation into the genome. To date, four globins (GLB‐1, GLB‐5, GLB‐6, and GLB‐26) have been partially characterized physicochemically, and the crystallographic structure of two of them (GLB‐1 and GLB‐6) was solved. In this article, a three‐dimensional model was designed for the other two globins (GLB‐5 and GLB‐26), and overlays of the globins were constructed to highlight the structural diversity among them. It is clear that although they all share the globin fold, small variations in the three‐dimensional structure have major implications on their ligand‐binding properties and possibly their function. We also review here all the information available so far on the globin family of C. elegans and suggest potential functions. © 2011 IUBMB IUBMB Life, 63(3): 166–174, 2011
Models, Molecular, 1303 Biochemistry, Protein Conformation, Molecular Sequence Data, 610 Medicine & health, 1308 Clinical Biochemistry, 10052 Institute of Physiology, 1307 Cell Biology, 1311 Genetics, 11554 Zurich Center for Integrative Human Physiology (ZIHP), 1312 Molecular Biology, Animals, Humans, Amino Acid Sequence, protein structure, Caenorhabditis elegans, Biology, Sequence Homology, Amino Acid, protein function, hemeproteins, Globins, oxgen metabolism, Chemistry, redox, 570 Life sciences; biology, Human medicine
Models, Molecular, 1303 Biochemistry, Protein Conformation, Molecular Sequence Data, 610 Medicine & health, 1308 Clinical Biochemistry, 10052 Institute of Physiology, 1307 Cell Biology, 1311 Genetics, 11554 Zurich Center for Integrative Human Physiology (ZIHP), 1312 Molecular Biology, Animals, Humans, Amino Acid Sequence, protein structure, Caenorhabditis elegans, Biology, Sequence Homology, Amino Acid, protein function, hemeproteins, Globins, oxgen metabolism, Chemistry, redox, 570 Life sciences; biology, Human medicine
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