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| | {{STRUCTURE_1sk3| PDB=1sk3 | SCENE= }} | | {{STRUCTURE_1sk3| PDB=1sk3 | SCENE= }} |
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| - | '''Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ialpha'''
| + | ===Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ialpha=== |
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| - | ==Overview==
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| - | Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors of the innate immune system that bind, and in some cases hydrolyze, peptidoglycans (PGNs) on bacterial cell walls. These molecules, which are highly conserved from insects to mammals, participate in host defense against both Gram-positive and Gram-negative bacteria. We report the crystal structure of the C-terminal PGN-binding domain of human PGRP-Ialpha in two oligomeric states, monomer and dimer, to resolutions of 2.80 and 1.65 A, respectively. In contrast to PGRPs with PGN-lytic amidase activity, no zinc ion is present in the PGN-binding site of human PGRP-Ialpha. The structure reveals that PGRPs exhibit extensive topological variability in a large hydrophobic groove, located opposite the PGN-binding site, which may recognize host effector proteins or microbial ligands other than PGN. We also show that full-length PGRP-Ialpha comprises two tandem PGN-binding domains. These domains differ at most potential PGN-contacting positions, implying different fine specificities. Dimerization of PGRP-Ialpha, which occurs through three-dimensional domain swapping, is mediated by specific binding of sodium ions to a flexible hinge loop, stabilizing the conformation found in the dimer. We further demonstrate sodium-dependent dimerization of PGRP-Ialpha in solution, suggesting a possible mechanism for modulating PGRP activity through the formation of multivalent adducts.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15140887}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15140887 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15140887}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Schuck, P.]] | | [[Category: Schuck, P.]] |
| | [[Category: Alpha/beta mix]] | | [[Category: Alpha/beta mix]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:48:16 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:27:08 2008'' |
Revision as of 00:27, 29 July 2008
Template:STRUCTURE 1sk3
Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ialpha
Template:ABSTRACT PUBMED 15140887
About this Structure
1SK3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the C-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein Ialpha., Guan R, Malchiodi EL, Wang Q, Schuck P, Mariuzza RA, J Biol Chem. 2004 Jul 23;279(30):31873-82. Epub 2004 May 12. PMID:15140887
Page seeded by OCA on Tue Jul 29 03:27:08 2008
