1-X-3 motif in inter-protein recognition: structures, widespreading and possible practical application.
Similarities in the discrete mode and size of contact areas of a wide range of protein complexes allows us to suggest the existence of a limited number of types of inter-protein interactions. Comparison of structures of bound determinants indicates that the double-module, 1-X-3 type of motif is widespread in recognition processes. Thus, in many cases, the sites of ligand recognition are formed by two significant amino acids and separated by insignificant ones. Typical examples of such motifs are the RGD sequence of some adhesive and haemostatic proteins, the primary sites for plasminogen sorption on the fibrin network, the reactive sites of protein inhibitors of serine proteinases, and the sites for activation of the hydrolysis of protein pro-forms and receptors. It is assumed that there is widespread double-module determinants in many inter-protein interactions.
Verevka
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The Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, 9 Leontovich Str., Kiev 01030, Ukraine. verevka@biochem.kiev.ua
Miroshnychenko
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D000327:Adsorption; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005337:Fibrin / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008024:Ligands; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D010958:Plasminogen / Q000737:chemistry; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D008024:Ligands; D009842:Oligopeptides; C047981:arginyl-glycyl-aspartic acid; D005337:Fibrin; D010958:Plasminogen