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4IM6

LRR domain from human NLRP1

Summary for 4IM6
Entry DOI10.2210/pdb4im6/pdb
DescriptorNACHT, LRR and PYD domains-containing protein 1, GLYCEROL (3 entities in total)
Functional Keywordslrr domain, ligand recognition, muramyl dipeptide, structural protein
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight22901.53
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 citationReubold, 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: 25064844
DOI: 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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건을2024-11-06부터공개중

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