Sandbox Reserved 1706: Difference between revisions

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<scene name='90/904312/Zoomed_lo/1'>(zoomed in)'</scene>.

==Domains==

===N-C HEAT ARM===

NF1 in its closed and open confirmations holds five separate domains. The first domain shown in black is representative of two separate but very similar domains, the N-HEAT ARM(N-Terminal) and C-HEAT ARM(C-Terminal). Structurally the N-HEAT Arm’s consists of various helices and loops that interconnect on one of the existing protomers. The N-HEAT ARM is critical in stabilization and linking the other domains which extend out from the core and are important to its catalytic function. The N-HEAT ARM in its linkage with the GRD catalytic domain, has a direct impact on the relative conformational change from the active (Ras BOUND) to inactive (Ras unbound) states. Finally, the Zn2+ binding site also exists downstream on the N-HEAT ARM just before the GRD and SEC14-PH domains. The C-HEAT Arm is linked structurally to the N-HEAT ARM and is a continuation of the protomer. It extends out on the opposing end from the other domains. In its structure consisting of various loops and helices, it is involved with stabilization and linking to the GRD and SEC14-PH and plays a role in the conformational changes from the closed to open state.

===GRD===

The GRD site is represented in cyan in all models. Neurofibromin’s main catalytic domain is the GRD active site. Linked structurally to both HEAT ARM’s, it consists of mainly loops and helices. Per protomer, there is one single GRD binding site. In the closed state Ras cannot bind due to a steric hindrance in which Ras clashes with the N-HEAT ARM upon attempting to bind to the GRD site. In its active state GRD can bind Ras. The critical residue within the GRD site is Arg1276.

Sandbox Reserved 1706: Difference between revisions

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@@ Line 26: / Line 26: @@
 <scene name='90/904312/Zoomed_lo/1'>(zoomed in)'</scene>.
 ==Domains==
+===N-C HEAT ARM===
+NF1 in its closed and open confirmations holds five separate domains. The first domain shown in black is representative of two separate but very similar domains, the N-HEAT ARM(N-Terminal) and C-HEAT ARM(C-Terminal). Structurally the N-HEAT Arm’s consists of various helices and loops that interconnect on one of the existing protomers. The N-HEAT ARM is critical in stabilization and linking the other domains which extend out from the core and are important to its catalytic function. The N-HEAT ARM in its linkage with the GRD catalytic domain, has a direct impact on the relative conformational change from the active (Ras BOUND) to inactive (Ras unbound) states. Finally, the Zn2+ binding site also exists downstream on the N-HEAT ARM just before the GRD and SEC14-PH domains. The C-HEAT Arm is linked structurally to the N-HEAT ARM and is a continuation of the protomer. It extends out on the opposing end from the other domains. In its structure consisting of various loops and helices, it is involved with stabilization and linking to the GRD and SEC14-PH and plays a role in the conformational changes from the closed to open state.
 ===GRD===
 The GRD site is represented in cyan in all models. Neurofibromin’s main catalytic domain is the GRD active site. Linked structurally to both HEAT ARM’s, it consists of mainly loops and helices. Per protomer, there is one single GRD binding site. In the closed state Ras cannot bind due to a steric hindrance in which Ras clashes with the N-HEAT ARM upon attempting to bind to the GRD site. In its active state GRD can bind Ras. The critical residue within the GRD site is Arg1276.