Modular Protein Structure Flashcards

1
Q

What is some evidence for parallel evolution (relating to proteins?)

A

A comparison of unrelated proteins with a similar structure

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2
Q

What is a protein sequence motif?

A

A pattern of amino acids that are found in related genes or proteins

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3
Q

What is a protein structure motif?

A

The structure of protein found in similar genes or proteins that don’t have similar primary structures

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4
Q

Where are motifs and domains commonly found?

A

Across functionally related proteins but may not be sequentially related?

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5
Q

What is a motif

A

Minimum arrangement Of independently forming secondary structures combining recognisable folds (arrangements) across many different proteins

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6
Q

What is a domain?

A

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

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7
Q

Both domains and motifs are what in nature?

A

Modular

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8
Q

What do domains often relate to?

A

A specific exon in a gene

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9
Q

How many different structural motifs exist?

A

1400-1500

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10
Q

What is an ef hand?

A

Ca2+ binding motif resembles a helix turn helix but combines with a metal ion.

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11
Q

Give two examples of ca2+ binding motifs

A

Calmodulin and troponin-C

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12
Q

What is calmodulin?

A

Part of a mechanism for sensing cellular calcium leads

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13
Q

What does the Greek key motif consist of?

A

Antiparallel beta strands forming a beta sheet

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14
Q

Why is the Greek key motif important?

A

It is such a common motif that isnt generally associated with a specific function

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15
Q

What is the beta- alpha- beta motif

A

Parallel strands of a beta sheet interlinked with an alpha helix. Beta strands are connected to an alpha strand which sits on top of the betas

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16
Q

What’s a beta barrel?

A

Beta strands wrapped around to form a circular tunnel

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17
Q

What is a DNA binding motif?

A

Helices inserted into the major groove of DNA in a sequence specific manner. Arranged to recognise specific DNA sequences

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18
Q

Give some examples of helix loop helix

A

Max and mad and ca2+ binding

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19
Q

Give some examples of helix turn helix

A

Cro, tryptophan and lac repressors

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20
Q

Give some examples of a leucine zipper

A

GCN4

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21
Q

Give some examples of a zinc finger

A

Hormone receptors

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22
Q

Give the most common example of a form of membrane bound receptors

A

Bundles of alpha helices

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23
Q

What is the most common arrangement of alpha helices in membrane bound receptors?

A

7-transmembrane arrangement

24
Q

Where is the 7-transmembrane arrangement of alpha helices found?

A

Rhodopsin, TSHr pharmacological receptors and some polypeptide hormone receptors

25
What are the membrane bound receptor domains called in the extracellular region?
Ligand binding domain
26
Where are the membrane bound receptor domains in the transmembrane region?
Domain embedded in the lipid bilayer
27
What does genome shuffling in the genome cause?
Modular units of function being conserved but shuttled between genes
28
What are the four different genes founds in mammalian phospholipids C?
Troponin C Bacterial phospholipase C Synaptotagmin Recoverin
29
How are myoglobin and haemoglobin similar and why?
Both have a tertiary structure, which suggests evolution from a common ancestral O2 binding polypeptide
30
What are transcription factors?
Proteins that bind to DNA and regulate transcription
31
What does each transcription factor contain a small number of?
Conserved motifs that combine to form domains that interact with the DNA
32
Are motifs different across phyla?
No, all conserved
33
What do DNA binding domains do?
Allow the regulatory function of their respective proteins
34
What is a recognition helix?
When an alpha helix fits inside the major groove of DNA
35
What does the amino acid sequence of a DNA binding motif provide?
Specificity
36
The helix-loop-helix motif only binds DNA in what form?
Dimeric
37
What are the two names for the dimers of the helix - loop - helix motif?
Heterodimer and homodimer
38
What is a homodimer?
Identical monomers
39
What is a heterodimer?
Different monomers
40
What is the central portion of the helix-loop-helix motif made from?
Overlapping helices that form a structure enabling dimerisation
41
What does the terminal part of the Lower opposing helices contain in the helix-loop-helix motif?
Basic amino acids that interact with the major groove of DNA- giving rise to the b/HLH functional domain
42
Give some examples of a helix-loop-helix motif
MAD, MAX, MYC, MYOD
43
What is the leucine zipper motif formed from?
2 contiguous alpha helices
44
What type of protein is the leucine zipper motif?
Dimeric
45
What do the dimers in the top stalk zip together to form?
A short coiled coil
46
How is the coil held together?
By hydrophobic interactions down opposing sides of the helix
47
What type of amino acids dominate the lower part of the helix
Basic
48
What does heterodimerisation do in the leucine zipper motif?
It expands with the regulatory potential of leucine zippers
49
What does the helix-turn-helix motif consist of?
Two short helices oriented at right angles to train each other - connected by a turn
50
Where is the helix-turn-helix found?
In both prokaryotic and eukaryotic DNA binding proteins
51
Give some examples of where the helix-turn-helix motif is found
CRO repressor and homeobox proteins
52
What is the CRO protein?
Homodimer
53
What does the CRO repressor do?
Recognises palindromic sequence and by binding DNA represses transcription
54
What is the zinc finger motif comprised of?
Alpha helix and beta sheet held together by non-covalent interactions with zinc
55
What does the alpha helix of each motif do with DNA in the zinc finger motif?
Knots with the major groove of the DNA and recognises specific DNA sequence
56
What hormones may have the zinc finger motifs in?
Glucorticoid Mineral corticoid Progesterone Vitamin D