title: Structural similarities and functional diversity of eukaryotic discoidin-like domains.
abstract: The discoidin domain is a approximately 150 amino acid motif common in both eukaryotic and prokaryotic proteins. It is found in a variety of extracellular, intracellular and transmembrane multidomain proteins characterized by a considerable functional diversity, mostly involved in developmental processes. The biological role of the domain depends on its interactions with different molecules, including growth factors, phospholipids and lipids, galactose or its derivatives, and collagen. The conservation of the motif, as well as the serious physiological consequences of discoidin domain disorders underscore the importance of the fold, while the ability to accommodate such an extraordinarily broad range of ligand molecules makes it a fascinating research target. In present review we characterize the distinctive features of discoidin domains and briefly outline the biological role of this module in various eukaryotic proteins.
authors: Faculty of Biotechnology, University of Wroclaw, Str. Tamka2, 50-137 Wroclaw, Poland.
authors: A
authors: A
authors: Kiedzierska
authors: K
authors: K
authors: Smietana
authors: H
authors: H
authors: Czepczynska
authors: J
authors: J
authors: Otlewski
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002268:Carboxypeptidases / Q000737:chemistry / Q000235:genetics; D015815:Cell Adhesion Molecules / Q000737:chemistry; D015816:Cell Adhesion Molecules, Neuronal / Q000737:chemistry; D000070818:Discoidin Domain Receptors; D000070821:Discoidins; D005136:Eye Proteins / Q000737:chemistry / Q000235:genetics; D005165:Factor V / Q000737:chemistry / Q000235:genetics; D005169:Factor VIII / Q000737:chemistry / Q000235:genetics; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry; D037102:Lectins / Q000737:chemistry* / Q000502:physiology; D008565:Membrane Proteins / Q000737:chemistry; D008958:Models, Molecular; D039921:Neuropilins / Q000737:chemistry / Q000502:physiology; D017434:Protein Structure, Tertiary; D015800:Protozoan Proteins / Q000737:chemistry* / Q000502:physiology; D020794:Receptor Protein-Tyrosine Kinases / Q000737:chemistry / Q000502:physiology; D011975:Receptors, Mitogen / Q000737:chemistry / Q000502:physiology; D012097:Repressor Proteins / Q000737:chemistry / Q000235:genetics; D016415:Sequence Alignment
chemical_list: C484818:AEBP1 protein, human; C491323:CNTNAP1 protein, human; D015815:Cell Adhesion Molecules; D015816:Cell Adhesion Molecules, Neuronal; D000070821:Discoidins; D005136:Eye Proteins; D047908:Intracellular Signaling Peptides and Proteins; D037102:Lectins; C503019:MKLN1 protein, human; D008565:Membrane Proteins; D039921:Neuropilins; D015800:Protozoan Proteins; C108726:RS1 protein, human; D011975:Receptors, Mitogen; D012097:Repressor Proteins; C477266:SED1 protein, mouse; D005165:Factor V; D005169:Factor VIII; D000070818:Discoidin Domain Receptors; D020794:Receptor Protein-Tyrosine Kinases; D002268:Carboxypeptidases