Modular structure of proteins Flashcards

1
Q

What is a structural motif

A

A minimum arrangement of independently forming secondary structures combining recognisable folds across many different proteins

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2
Q

How does a motif and domain differ

A

A domain more clearly defines a functional unit

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3
Q

How are motifs and domains similar

A

both are modular in nature and both are evolutionarily conserved

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4
Q

What is a domain

A

A complex structure at the tertiary or quaternary level, often involving interaction between distant parts of a protein or motifs

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5
Q

EF hand motif

A

Calcium binding motif
Resembles a helix turn helix with a metal ion such as calcium that stabilises the overall structure
Calmodulin has 4 EF hand motifs

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6
Q

Greek key motif

A

Consists of antiparallel beta strands that generally isnt associated with a specific function

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7
Q

Beta barrel motif

A

Beta strands forming beta sheets which are wrapped around to form a circular tunnel

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8
Q

Beta-alpha-beta motif

A

Two parallel strands of a beta sheet interlinked with an alpha helix

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9
Q

What are DNA binding motifs

A

They are helices which can be inserted into the major groove of DNA, often dimerise creating a a larger and more complex DNA binding domain

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10
Q

What is a membrane bound receptor domain

A

Bundles of alpha helices or beta sheets

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11
Q

What is the extracellular region

A

ligand binding domain

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12
Q

What is the transmembrane region

A

Domain that anchors the protein to the membrane and embeds it into the lipid bilayer

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13
Q

What is the intracellular region

A

Domain that interacts with the interior of the cell or organelle relaying the signal

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14
Q

What does domain shuffling achieve

A

Results in modular units of function being evolutionarily conserved

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15
Q

Helix-loop-helix motif structure and function

A
  • DNA binding motif in the dimeric form
  • Central portion formed from overlapping helices that allow for dimerisation
  • Terminal parts contain basic amino acids that interact with the positively charged major groove of DNA
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16
Q

What is the advantage of helix-loop-helix motifs being able to form heterodimers

A

Extends the functionality of individual proteins as different monomers can join together allowing the regulation of different genes in different ways in response to different stimuli

17
Q

Leucine zipper motif structure

A

Formed from 2 contiguous alpha helices, the dimers zip together forming a coil a the top
The coil is held together by hydrophobic interactions down opposing sides of the helix
The basic amino acids are also on the lower part of the helix

18
Q

Helix-turn-helix structure

A

Consists of two short helices oriented at right angles to each others and connected by a ‘turn’

19
Q

Where are H-T-H found

A

In eukaryotic and prokaryotic DNA binding poteins e.g. CRO repressor and homebox proteins

20
Q

What does the CRO repressor do

A

Recognises palindromic sequences and binding to the DNA it represses transcription

21
Q

Zinc finger motif

A

It is an alpha helix and a beta sheet held together by non-covalent interactions with zinc

22
Q

Where do you find zinc finger motive

A

In manu ornate receptors e.g. glucocorticoid, mineralocorticoid, oestrogen, progesterone and vit D receptors