Title : The structure of the NPC1L1 N-terminal domain in a closed conformation.

Pub. Date : 2011 Apr 15

PMID : 21525977






3 Functional Relationships(s)
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1 Comparison to the cholesterol free and bound structures of NPC1(NTD) reveals that NPC1L1(NTD) is in a closed conformation and the sterol binding pocket is occluded from solvent. Sterols NPC1 like intracellular cholesterol transporter 1 Homo sapiens
2 CONCLUSION: The structure of NPC1L1(NTD) reveals a degree of flexibility surrounding the entrance to the sterol binding pocket, suggesting a gating mechanism that relies on multiple movements around the entrance to the sterol binding pocket. Sterols NPC1 like intracellular cholesterol transporter 1 Homo sapiens
3 CONCLUSION: The structure of NPC1L1(NTD) reveals a degree of flexibility surrounding the entrance to the sterol binding pocket, suggesting a gating mechanism that relies on multiple movements around the entrance to the sterol binding pocket. Sterols NPC1 like intracellular cholesterol transporter 1 Homo sapiens