1xfe
From Proteopedia
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'''Solution structure of the LA7-EGFA pair from the LDL receptor''' | '''Solution structure of the LA7-EGFA pair from the LDL receptor''' | ||
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[[Category: Fisher, C.]] | [[Category: Fisher, C.]] | ||
[[Category: Jeon, H.]] | [[Category: Jeon, H.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:57:31 2008'' | |
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Revision as of 11:57, 3 May 2008
Solution structure of the LA7-EGFA pair from the LDL receptor
Contents |
Overview
Low-density lipoprotein (LDL) receptors bind lipoprotein particles at the cell surface and release them in the low pH environment of the endosome. The published structure of the receptor determined at endosomal pH reveals an interdomain interface between its beta propeller and its fourth and fifth ligand binding (LA) repeats, suggesting that the receptor adopts a closed conformation at low pH to release LDL. Here, we combine lipoprotein binding and release assays with NMR spectroscopy to examine structural features of the receptor promoting release of LDL at low pH. These studies lead to a model in which the receptor uses a pH-invariant scaffold as an anchor to restrict conformational search space, combining it with flexible linkers between ligand binding repeats to interconvert between open and closed conformations. This finely tuned balance between interdomain rigidity and flexibility is likely to represent a shared structural feature in proteins of the LDL receptor family.
Disease
Known disease associated with this structure: Hypercholesterolemia, familial OMIM:[606945]
About this Structure
1XFE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Cooperation between fixed and low pH-inducible interfaces controls lipoprotein release by the LDL receptor., Beglova N, Jeon H, Fisher C, Blacklow SC, Mol Cell. 2004 Oct 22;16(2):281-92. PMID:15494314 Page seeded by OCA on Sat May 3 14:57:31 2008
