2fcw
From Proteopedia
(New page: 200px<br /> <applet load="2fcw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fcw, resolution 1.26Å" /> '''Structure of a Comp...) |
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| - | [[Image:2fcw.gif|left|200px]]<br /> | + | [[Image:2fcw.gif|left|200px]]<br /><applet load="2fcw" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2fcw" size=" | + | |
caption="2fcw, resolution 1.26Å" /> | caption="2fcw, resolution 1.26Å" /> | ||
'''Structure of a Complex Between the Pair of the LDL Receptor Ligand-Binding Modules 3-4 and the Receptor Associated Protein (RAP).'''<br /> | '''Structure of a Complex Between the Pair of the LDL Receptor Ligand-Binding Modules 3-4 and the Receptor Associated Protein (RAP).'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Proteins of the low-density lipoprotein receptor (LDLR) family are | + | Proteins of the low-density lipoprotein receptor (LDLR) family are remarkable in their ability to bind an extremely diverse range of protein and lipoprotein ligands, yet the basis for ligand recognition is poorly understood. Here, we report the 1.26 A X-ray structure of a complex between a two-module region of the ligand binding domain of the LDLR and the third domain of RAP, an escort protein for LDLR family members. The RAP domain forms a three-helix bundle with two docking sites, one for each LDLR module. The mode of recognition at each site is virtually identical: three conserved, calcium-coordinating acidic residues from each LDLR module encircle a lysine side chain protruding from the second helix of RAP. This metal-dependent mode of electrostatic recognition, together with avidity effects resulting from the use of multiple sites, represents a general binding strategy likely to apply in the binding of other basic ligands to LDLR family proteins. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FCW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, NA and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2FCW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Beglova, N.]] | [[Category: Beglova, N.]] | ||
| - | [[Category: Blacklow, S | + | [[Category: Blacklow, S C.]] |
[[Category: Fisher, C.]] | [[Category: Fisher, C.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: rap]] | [[Category: rap]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:07 2008'' |
Revision as of 15:20, 21 February 2008
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Structure of a Complex Between the Pair of the LDL Receptor Ligand-Binding Modules 3-4 and the Receptor Associated Protein (RAP).
Contents |
Overview
Proteins of the low-density lipoprotein receptor (LDLR) family are remarkable in their ability to bind an extremely diverse range of protein and lipoprotein ligands, yet the basis for ligand recognition is poorly understood. Here, we report the 1.26 A X-ray structure of a complex between a two-module region of the ligand binding domain of the LDLR and the third domain of RAP, an escort protein for LDLR family members. The RAP domain forms a three-helix bundle with two docking sites, one for each LDLR module. The mode of recognition at each site is virtually identical: three conserved, calcium-coordinating acidic residues from each LDLR module encircle a lysine side chain protruding from the second helix of RAP. This metal-dependent mode of electrostatic recognition, together with avidity effects resulting from the use of multiple sites, represents a general binding strategy likely to apply in the binding of other basic ligands to LDLR family proteins.
Disease
Known disease associated with this structure: Hypercholesterolemia, familial OMIM:[606945]
About this Structure
2FCW is a Protein complex structure of sequences from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors., Fisher C, Beglova N, Blacklow SC, Mol Cell. 2006 Apr 21;22(2):277-83. PMID:16630895
Page seeded by OCA on Thu Feb 21 17:20:07 2008
Categories: Homo sapiens | Protein complex | Beglova, N. | Blacklow, S C. | Fisher, C. | CA | MPD | NA | Calcium-binding | Escort protein | Ldlr | Protein-protein complex | Rap
