Modular Structure of Proteins Flashcards

1
Q

what is a motif?

A

the minimum arrangement of independently forming 2° structures combining recognisable folds across many different proteins

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2
Q

how are motifs organised?

A

organised into lager structural and functional domains

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3
Q

what are domains?

A

more a more defined functional unit than a motif

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4
Q

what is the function of domains?

A

usually they are responsible for a particular function or interaction, contributing to the overall role of a protein.

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5
Q

how many structural motifs exist?

A

1400-1500

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6
Q

what are some examples of motifs?

A
  • EF hand

- Greek key

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7
Q

what are the functions of DNA binding motifs?

A

arranged to recognise specific sequence of bases

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8
Q

what are examples of DNA binding motifs?

A
  • helix-loop-helix
  • helix-turn-helix
  • leucine zipper
  • zinc finger
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9
Q

what do all DNA binding motifs have in common?

A

all have α helices that are inserted into the major groove of the DNA sequence in a specific manner

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10
Q

what are properties of the EF hand motif? and give an example

A
  • resembles alpha helix-turn-helix
  • but combines with a metal ion such as calcium

-(eg. Calmodulin, Troponin, etc. Calmodulin contains four EF hands, each binding to a single calcium ion)

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11
Q

what are properties of a greek key motif?

A
  • consist of antiparallel β strands

- motif that is so common that it isn’t generally associated with a specific function

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12
Q

what is domain shuffling?

A

-domain shuffling is where gene segments coding for functional domains are shuffled between different genes during evolution

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13
Q

what do transcription factors have in common across eukaryotes?

A
  • there are many different transcription factors but they each contain a small number of conserved motifs which combine to form domains that interact with the DNA.
  • these motifs are conserved across all phyla (ie huge variety of eukaryotes, ranging from fungi to plants and animals).
  • these motifs form DNA binding domains that allow the regulatory function of their respective proteins.
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14
Q

explain the importance of α helices

A
  • can fit in major groove of DNA
  • aa sequence of DNA binding motif provides specificity
  • diff DNA binding domains and. motifs present binding helix using diff arrangements of structural motifs
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15
Q

give some properties of the helix loop helix motif including what the central and terminal parts are made of and give examples

A
  • binds to DNA in dimeric form
  • exists as hetero- (different monomers) or homodimers (same monomer)
  • central portion made of overlapping helices that form structure to enable dimerisation
  • terminal part of opposing helices have basic aa that interact w major groove of DNA
    eg: mad, max, myc, myoD
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16
Q

describe the leucine zipper motif

A
  • resembles helix-loop-helix but formed from 2 contiguous α helices and dimeric protein formed form 2 polypeptides
  • dimers ‘zip’ together in top ‘stalk’ to form short coiled coil
  • basic aa dominate lower part of helix and interact w major groove
  • heterodimerisation expands regulatory potential of leucine zippers
    eg: cFos, cJun
17
Q

describe the helix loop helix

A
  • 2 short helices oriented at 90 ° and connected by ‘turn’
  • found in prok. + euk. DNA binding proteins
  • only recognition helix interacts w nucleotide sequence and locates within major groove
    eg: CRO, lambda repressors
18
Q

what does the CRO repressor do?

A
  • is a homodimer

- recognises palindromic sequence by binding to DNA and repressing transcription

19
Q

describe the zinc finger motif

A
  • α helix nad β sheet held together by non-covalent interactions w Zn
  • α helix of each motif interacts w major groove and recognises specific DNA sequence
  • other parts of dimer contributes to DNA binding domain in addition to each of the motifs
  • other parts form diff functions domains
    eg: glucocorticoid, progesterone, vitamin D