1ajj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1ajj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ajj, resolution 1.7&Aring;" /> '''LDL RECEPTOR LIGAND-...)
Line 1: Line 1:
-
[[Image:1ajj.gif|left|200px]]<br />
+
[[Image:1ajj.gif|left|200px]]<br /><applet load="1ajj" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1ajj" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1ajj, resolution 1.7&Aring;" />
caption="1ajj, resolution 1.7&Aring;" />
'''LDL RECEPTOR LIGAND-BINDING MODULE 5, CALCIUM-COORDINATING'''<br />
'''LDL RECEPTOR LIGAND-BINDING MODULE 5, CALCIUM-COORDINATING'''<br />
==Overview==
==Overview==
-
The low-density lipoprotein receptor (LDLR) is responsible for the uptake, of cholesterol-containing lipoprotein particles into cells. The, amino-terminal region of LDLR, which consists of seven tandemly repeated, approximately 40-amino-acid, cysteine-rich modules (LDL-A modules), mediates binding to lipoproteins. LDL-A modules are biologically, ubiquitous domains, found in over 100 proteins in the sequence database., The structure of ligand-binding repeat 5 (LR5) of the LDLR, determined to, 1.7 A resolution by X-ray crystallography and presented here, contains a, calcium ion coordinated by acidic residues that lie at the, carboxy-terminal end of the domain and are conserved among LDL-A modules., Naturally occurring point mutations found in patients with the disease, familial hypercholesterolaemia alter residues that directly coordinate, Ca2+ or that serve as scaffolding residues of LR5.
+
The low-density lipoprotein receptor (LDLR) is responsible for the uptake of cholesterol-containing lipoprotein particles into cells. The amino-terminal region of LDLR, which consists of seven tandemly repeated, approximately 40-amino-acid, cysteine-rich modules (LDL-A modules), mediates binding to lipoproteins. LDL-A modules are biologically ubiquitous domains, found in over 100 proteins in the sequence database. The structure of ligand-binding repeat 5 (LR5) of the LDLR, determined to 1.7 A resolution by X-ray crystallography and presented here, contains a calcium ion coordinated by acidic residues that lie at the carboxy-terminal end of the domain and are conserved among LDL-A modules. Naturally occurring point mutations found in patients with the disease familial hypercholesterolaemia alter residues that directly coordinate Ca2+ or that serve as scaffolding residues of LR5.
==Disease==
==Disease==
Line 11: Line 10:
==About this Structure==
==About this Structure==
-
1AJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AJJ OCA].
+
1AJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AJJ OCA].
==Reference==
==Reference==
Line 17: Line 16:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Berger, J.M.]]
+
[[Category: Berger, J M.]]
-
[[Category: Blacklow, S.C.]]
+
[[Category: Blacklow, S C.]]
[[Category: Fass, D.]]
[[Category: Fass, D.]]
-
[[Category: Kim, P.S.]]
+
[[Category: Kim, P S.]]
[[Category: CA]]
[[Category: CA]]
[[Category: SO4]]
[[Category: SO4]]
Line 28: Line 27:
[[Category: receptor]]
[[Category: receptor]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:59:13 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:13 2008''

Revision as of 09:45, 21 February 2008

Image:1ajj.gif

1ajj, resolution 1.7Å

Drag the structure with the mouse to rotate

LDL RECEPTOR LIGAND-BINDING MODULE 5, CALCIUM-COORDINATING

Contents

Overview

The low-density lipoprotein receptor (LDLR) is responsible for the uptake of cholesterol-containing lipoprotein particles into cells. The amino-terminal region of LDLR, which consists of seven tandemly repeated, approximately 40-amino-acid, cysteine-rich modules (LDL-A modules), mediates binding to lipoproteins. LDL-A modules are biologically ubiquitous domains, found in over 100 proteins in the sequence database. The structure of ligand-binding repeat 5 (LR5) of the LDLR, determined to 1.7 A resolution by X-ray crystallography and presented here, contains a calcium ion coordinated by acidic residues that lie at the carboxy-terminal end of the domain and are conserved among LDL-A modules. Naturally occurring point mutations found in patients with the disease familial hypercholesterolaemia alter residues that directly coordinate Ca2+ or that serve as scaffolding residues of LR5.

Disease

Known disease associated with this structure: Hypercholesterolemia, familial OMIM:[606945]

About this Structure

1AJJ is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module., Fass D, Blacklow S, Kim PS, Berger JM, Nature. 1997 Aug 14;388(6643):691-3. PMID:9262405

Page seeded by OCA on Thu Feb 21 11:45:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ajj"
Personal tools