4IM6
LRR domain from human NLRP1
Summary for 4IM6
Entry DOI | 10.2210/pdb4im6/pdb |
Descriptor | NACHT, LRR and PYD domains-containing protein 1, GLYCEROL (3 entities in total) |
Functional Keywords | lrr domain, ligand recognition, muramyl dipeptide, structural protein |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 1 |
Total formula weight | 22901.53 |
Authors | Hahne, G.,Reubold, T.F.,Eschenburg, S. (deposition date: 2013-01-02, release date: 2014-01-08, Last modification date: 2024-10-16) |
Primary citation | Reubold, T.F.,Hahne, G.,Wohlgemuth, S.,Eschenburg, S. Crystal structure of the leucine-rich repeat domain of the NOD-like receptor NLRP1: implications for binding of muramyl dipeptide. Febs Lett., 588:3327-3332, 2014 Cited by PubMed Abstract: The NOD-like receptor NLRP1 (NLR family, pyrin domain containing 1) senses the presence of the bacterial cell wall component l-muramyl dipeptide (MDP) inside the cell. We determined the crystal structure of the LRR domain of human NLRP1 in the absence of MDP to a resolution of 1.65Å. The fold of the structure can be assigned to the ribonuclease inhibitor-like class of LRR proteins. We compared our structure with X-ray models of the LRR domains of NLRX1 and NLRC4 and a homology model of the LRR domain of NOD2. We conclude that the MDP binding site of NLRP1 is not located in the LRR domain. PubMed: 25064844DOI: 10.1016/j.febslet.2014.07.017 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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