modular structure of proteins Flashcards
Motifs and domains
Simple secondary structures fold combine to form structural motifs or larger functional domains
Independent order of structure Commonly found and conserved across functionally related proteins
Motifs
Combination of two or more secondary structures to form a recognizable folded arrangement
Organized or combined into larger structural and functional domains EF hand is a motif which allows the binding of Ca2+ Resembles a helix turn helix Greek key motif: Consists of antiparallel beta strands Forms easily during protein folding process Therefore common and generally isn’t associated with a specific function Beta barrel: Beta strand wrap around to form circular tunnel
Domains
Complex structure at the tertiary or quaternary level often involving interactions between distant parts of a protein or motifs
Globin domain
Each chain of HB has a very similar tertiary structure to a single myoglobin chain
This strongly suggests evolution from a common ancestral O2 binding polypeptide
DNA binding motifs
Helices can be inserted into the major groove of DNA in a sequence specific matter
Amino acid sequence of a DNA binding motif provides specificity
DNA binding motifs (Helix loop helix)
Found in some transcription factors
Central portion is made from overlapping helices that form a structure enabling dimerization Larger helix contains the DNA binding regions Terminal part of the lower opposing helices contain basic amino acids that interact with the major groove of the DNA – giving rise to b/HLH functional domain
DNA binding motifs (Leucine zipper)
Formed from 2 contiguous alpha helices and is a dimeric protein formed from two polypeptide chains
Dimers zip together in the top stalk to form a short coiled coil Coil held together by hydrophobic interactions down opposing sides of the helix Basic amino acid dominate lower part of the helix and interact with the DNA major groove Heterodimersation expands the regulatory potential of leucine zippers
DNA binding motifs (Helix turn helix)
Two short helices orientated at right angles to each other and connected by a turn
Motif found in both eukaryotic and prokaryotic DNA binding proteins CRO is a homodomer Recognizes palindromic sequence and by binding DNA represses transcription Only recognition helix interacts with nucleotide sequence and locates within the major groove
DNA binding motifs (zinc finger)
Alpha helix and beta sheet held together by non-covalent interactions with zinc
Alpha helix of each motif interacts with the major groove of DNA and recognizes a specific DNA sequence Present in many hormone receptors