COMPLEMENT me please Flashcards

1
Q

Basic description of the complement system if u please

A

Front line of defence, evolved to be more sophisticated like my style NOT, interacts with other systems, ANCIENT, aberrant activation/deficiency = disease

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2
Q

What are the names of the three complement pathways?

A

Classical, alternative and lectin baby

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3
Q

Briefly describe the classical pathway

A

C1 binding to immune complexes, including antibodies and c-reactive protein ab dependent pathway

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4
Q

Briefly describe the alternative pathway

A

C3 binds to susceptible foreign surfaces eg bac and yeast cell walls

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5
Q

Briefly describe the lectin pathway

A

Lectin binding to carbs on microbial surfaces - ANCIENT

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6
Q

Define C1q

A

recognises and binds opsonins (antibodies and C reactive protein, which must be antigen bound for recognition.)

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7
Q

Where is the antibody binding site of C1q?

A

In the globular head

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8
Q

Where do non-immune activators of classical pathway bind?

A

The collagen-like tail. They also activate it.

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9
Q

Where is the CRP binding site?

A

In the collagen region. Maybe.

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10
Q

DRAW C1q + SERINE PROTEASES C1r and C1s

A

go girl g g go go go

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11
Q

What is ACRP30? And why, oh why, is it mentioned in the here and now?

A

An adipose specific protein in obese mice/human. Participates in energy homeostasis. It’s a homotrimer of beta-sandwich protomers, each of which has a 10 strand jelly roll folding topology, similar to TNF family. Mentioned because it is a module similar to the globular heads of C1q

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12
Q

What is collagen X NC1? And why is it mentioned?

A

Collagen X NC1 domain trimer, non collagenous. expressed in growth plate of long bones. C1q like C-terminal NC1 domain crucial for collagen X assembly. Mentioned b/c it is a module similar to the globular heads of C1q.

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13
Q

Name two modules similar to the globular heads of C1q

A

ACRP30 and Collagen X NC1

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14
Q

Describe the crystal structure of C1q trimer

A

Same fold as ACRP30 and Collagen X NC1 domain trimer. 3 distinct chains, A B and C. the differences in amino acids and structure probably reflect the different binding properties of each C1q chain.

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15
Q

NOW, ABOUT THE RECOGNITION PROPERTIES OF C1q. What kind of ‘imer’ is it? Describe the structure.

A

A heterotrimer. An overlay of subunits, strong conservation of beta strands and significant variability in loops. Different charged and hydrophobic residues on surface, could reflect specific individual recognition properties.

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16
Q

Go on about C1q’s interaction with IgG

A

IgG b12 has extreme flexibility, so its Fab arm variably binds to C1q’s binding site and its Fc region invariably.