2fcw: Difference between revisions

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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="~~450~~" color="white" frame="true" align="right" spinBox="true"

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 />

==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.

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==

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==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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2FCW OCA].

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==

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[[Category: Protein complex]]

[[Category: Beglova, N.]]

[[Category: Blacklow, S.C.]]

[[Category: Blacklow, S C.]]

[[Category: Fisher, C.]]

[[Category: CA]]

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[[Category: rap]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 22~~:03:~~31 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:07 2008''

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@@ Line 1: / Line 1: @@
-[[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="450" color="white" frame="true" align="right" spinBox="true"
 caption="2fcw, resolution 1.26&Aring;" />
 '''Structure of a Complex Between the Pair of the LDL Receptor Ligand-Binding Modules 3-4 and the Receptor Associated Protein (RAP).'''<br />
 ==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.
+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==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-FCW 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FCW OCA].
+FCW 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==
@@ Line 18: / Line 17: @@
 [[Category: Protein complex]]
 [[Category: Beglova, N.]]
-[[Category: Blacklow, S.C.]]
+[[Category: Blacklow, S C.]]
 [[Category: Fisher, C.]]
 [[Category: CA]]
@@ Line 29: / Line 28: @@
 [[Category: rap]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:03:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:07 2008''