1TWQ
Crystal structure of the C-terminal PGN-binding domain of human PGRP-Ialpha in complex with PGN analog muramyl tripeptide
Summary for 1TWQ
| Entry DOI | 10.2210/pdb1twq/pdb |
| Related | 1SK3 1SK4 |
| Descriptor | peptidoglycan recognition protein-I-alpha, muramyl tripeptide, NICKEL (II) ION, ... (5 entities in total) |
| Functional Keywords | crystal structure; complex; pgrp; pgrp-ialpha; pgn analog, immune system, membrane protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 18968.17 |
| Authors | Guan, R.,Roychowdury, A.,Boons, G.-A.,Mariuzza, R.A. (deposition date: 2004-07-01, release date: 2004-12-14, Last modification date: 2024-02-28) |
| Primary citation | Guan, R.,Roychowdhury, A.,Ember, B.,Kumar, S.,Boons, G.-A.,Mariuzza, R.A. Structural basis for peptidoglycan binding by peptidoglycan recognition proteins Proc.Natl.Acad.Sci.USA, 101:17168-17173, 2004 Cited by PubMed Abstract: Peptidoglycan (PGN) recognition proteins (PGRPs) are pattern-recognition receptors of the innate immune system that bind and, in some cases, hydrolyze bacterial PGNs. We determined the crystal structure, at 2.30-A resolution, of the C-terminal PGN-binding domain of human PGRP-Ialpha in complex with a muramyl tripeptide representing the core of lysine-type PGNs from Gram-positive bacteria. The peptide stem of the ligand is buried at the deep end of a long binding groove, with N-acetylmuramic acid situated in the middle of the groove, whose shallow end can accommodate a linked N-acetylglucosamine. Although most interactions are with the peptide, the glycan moiety also seems to be essential for specific recognition by PGRPs. Conservation of key PGN-contacting residues shows that all PGRPs employ this basic PGN-binding mode. The structure pinpoints variable residues that likely mediate discrimination between lysine- and diaminopimelic acid-type PGNs. We also propose a mechanism for PGN hydrolysis by Zn(2+)-containing PGRPs. PubMed: 15572450DOI: 10.1073/pnas.0407856101 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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