Sandbox Reserved 595: Difference between revisions
No edit summary |
No edit summary |
||
| Line 11: | Line 11: | ||
<Structure load='1NFN' size='500' frame='true' align='right' caption='3-D Rendering of ApoE3 N-terminus' scene='Insert optional scene name here' /> | <Structure load='1NFN' size='500' frame='true' align='right' caption='3-D Rendering of ApoE3 N-terminus' scene='Insert optional scene name here' /> | ||
==Primary Structural Features== | ==Primary Structural Features== | ||
Apolipoprotein E is a polymorphic glycoprotein that consists of 299 amino acids (A,F). It has a molecular weight of 34kDa (G). The primary structure for ApoE is rich in the amino acid | Apolipoprotein E is a polymorphic glycoprotein that consists of 299 amino acids (A,F). It has a molecular weight of 34kDa (G). The primary structure for ApoE is rich in the amino acid <scene name='Sandbox_Reserved_595/Arginine/1'>arginine</scene> | ||
ApoE folds into two independent structural domains that are connected via a hinge region (A,F,M). The amino-terminal domain has a molecular weight of 2kDa and is comprised of the amino acid residues 1-199 (C,F,J,M). It is a globular domain consisting of an antiparallel bundle of 4 amphipathic <scene name='Sandbox_Reserved_595/4-helix_bundle/1'>alpha-helices</scene>, rich in basic amino acids; pronounced kinks are present in the helices near the end of the 4-helix bundle that correspond with the protein's lipid binding ability (C,F,J,L). In the fourth helix, the residues between 134-150, known as the <scene name='Sandbox_Reserved_595/Ldl-r_binding_region/1'>low density lipoprotein receptor binding region</scene>, are responsible for ApoE's ability to bind to members of the LDL receptor family (C,F,J,L). This domain also contains the variable <scene name='Sandbox_Reserved_595/Residues_112_and_158/3'>residues 112 and 158</scene> (112 blue & 158 in red), which are responsible for much of the differences between the three isoforms of apoE. | ApoE folds into two independent structural domains that are connected via a hinge region (A,F,M). The amino-terminal domain has a molecular weight of 2kDa and is comprised of the amino acid residues 1-199 (C,F,J,M). It is a globular domain consisting of an antiparallel bundle of 4 amphipathic <scene name='Sandbox_Reserved_595/4-helix_bundle/1'>alpha-helices</scene>, rich in basic amino acids; pronounced kinks are present in the helices near the end of the 4-helix bundle that correspond with the protein's lipid binding ability (C,F,J,L). In the fourth helix, the residues between 134-150, known as the <scene name='Sandbox_Reserved_595/Ldl-r_binding_region/1'>low density lipoprotein receptor binding region</scene>, are responsible for ApoE's ability to bind to members of the LDL receptor family (C,F,J,L). This domain also contains the variable <scene name='Sandbox_Reserved_595/Residues_112_and_158/3'>residues 112 and 158</scene> (112 blue & 158 in red), which are responsible for much of the differences between the three isoforms of apoE. | ||