Chapter 10 - Protein Domains and Binding Targets

Question 1

a polypeptide sequence of ~35-250 amino acids that folds independently into a functional unit

Answer 1

domain

Question 2

protein domains that mediate interactions with other molecules within the cell

Answer 2

interaction domains

Question 3

protein domains that catalyze enzymatic reactions

Answer 3

catalytic domains

Question 4

multiple domains which are joined by less ordered linker sequences

Answer 4

modular domains

Question 5

What are the three key structures which clobular domains organizes?

Answer 5

• hydrophobic amino acids
• binding or catalytic residues
• key residues

Question 6

what kind of amino acids are involved in binding or catalysis?

Answer 6

conserved amino acids

Question 7

what kind of amino acids dictate binding specificity?

Answer 7

variable residues

Question 8

In an interaction domain, where are the N and C termini usually located in relation to each other as well as the ligand binding pocket?

Answer 8

• usually found close to each other
• opposite side of the binding pocket

Question 9

binding target?

14-3-3

Answer 9

phosphoserine/phosphothreonine
(pSer, pThr)

Question 10

binding target?

ANK

Answer 10

repeat domain, diverse BPs

Question 11

binding target?

ANTH/CALM

Answer 11

phospholipids

Question 12

binding target?

ARM

Answer 12

repeat domain, diverse BPs

Question 13

binding target?

BAR

Answer 13

dimerization, lipids, and curved surfaces

Question 14

binding targets?

BEACH

Answer 14

phospholipids

Question 15

biding targets?

BH1-BH4

Answer 15

dimerization

Question 16

binding target?

BIR

Answer 16

repeat domain, caspases

Question 17

binding target?

BRCT

Answer 17

phosphoserine/phosphothreonine
(pSer, pThr)

Question 18

binding target?

Bromo

Answer 18

acetyl-lysine