C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer.
about
Crystallographic Insights into the Autocatalytic Assembly Mechanism of a Bacteriophage Tail SpikeCrystal Structure of Human Collagen XVIII Trimerization Domain: A Novel Collagen Trimerization FoldNonnative interactions between cysteines direct productive assembly of P22 tailspike protein.The C-terminus of the P22 tailspike protein acts as an independent oligomerization domain for monomeric proteins.Three amino acids that are critical to formation and stability of the P22 tailspike trimer.Buried hydrophobic side-chains essential for the folding of the parallel beta-helix domains of the P22 tailspike.Characterization of a novel intramolecular chaperone domain conserved in endosialidases and other bacteriophage tail spike and fiber proteins.
P2860
Q27655503-9628734E-8216-4F99-8B29-7E1EC7BAF6D1Q27656720-AF06BF4B-99AC-4428-A050-17E9B5615E64Q34183606-33E89704-CB04-4D35-A995-FE8107A5C31DQ36032778-90FDFFAB-023E-47F9-A4F9-2A0E8BF50E19Q41323984-8F76392D-AD6C-44D8-A845-369D878483FEQ41862592-684F8928-BBF4-4215-8536-50DD2C96A25EQ53583830-391D6F2B-FEDD-41D4-89F9-5045CDC2124B
P2860
C-terminal hydrophobic interactions play a critical role in oligomeric assembly of the P22 tailspike trimer.
description
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2003年の論文
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@zh-hk
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name
C-terminal hydrophobic interac ...... y of the P22 tailspike trimer.
@en
type
label
C-terminal hydrophobic interac ...... y of the P22 tailspike trimer.
@en
prefLabel
C-terminal hydrophobic interac ...... y of the P22 tailspike trimer.
@en
P2860
P356
P1433
P1476
C-terminal hydrophobic interac ...... ly of the P22 tailspike trimer
@en
P2093
Matthew J Gage
P2860
P304
P356
10.1110/PS.03150303
P577
2003-12-01T00:00:00Z