SARM1: Difference between revisions

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== Function ==
== Function ==


'''SARM1''' or '''NAD(+) hydrolase''' or '''sterile alpha and TIR motif-containing protein 1''' or '''NADase''' is a NAD-cleaving enzyme whose activation triggers axon destruction. SARM1 is a metabolic sensor responding to an increased NMN/NAD+ ratio by cleaving residual NAD+ and inducing axonal demise<ref>PMID:33657413</ref>. SARM1-induced axon destruction can be counteracted by increased NAD+ synthesis<ref>PMID:25908823</ref>.
'''SARM1''' or '''NAD(+) hydrolase''' or '''sterile alpha and TIR motif-containing protein 1''' or '''NADase''' is a NAD-cleaving enzyme whose activation triggers axon destruction. SARM1 is a metabolic sensor responding to an increased NMN/NAD+ ratio by cleaving residual NAD+ and inducing axonal demise<ref>PMID:33657413</ref>. SARM1-induced axon destruction can be counteracted by increased NAD+ synthesis<ref>PMID:25908823</ref>.


== Disease ==
== Disease ==
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== Structural highlights ==
== Structural highlights ==


The 3D structure of SARM1 shows the octamer structure with outer ring dimension of 200A, inner ring of 45A and thickness of 60A<ref>PMID:33053563</ref>. The 3 domains of SARM1 are ARM, SAM and TIR.  The interaction of the ARM and TIR domains cause the autoinhibition of SARM1. NAD(+) binding pocket is at the concave side of the ARM domain.
The 3D structure of SARM1 shows the <scene name='91/918463/Cv/2'>octamer structure</scene> with outer ring dimension of 200A, inner ring of 45A and thickness of 60A<ref>PMID:33053563</ref>. The 3 domains of SARM1 are ARM, SAM and TIR.  The interaction of the ARM and TIR domains cause the autoinhibition of SARM1. NAD(+) binding pocket is at the concave side of the ARM domain.
==3D structures of SARM1==
==3D structures of SARM1==
[[SARM1 3D structures]]
[[SARM1 3D structures]]

Revision as of 10:03, 3 August 2022

Human SARM1 complex with NAD(+) (PDB ID 7cm6).

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References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky