3ln2
From Proteopedia
Contents |
Crystal Structure of a Charge Engineered Human Lysozyme Variant
Template:ABSTRACT PUBMED 21408218
Disease
[LYSC_HUMAN] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.[1]
Function
[LYSC_HUMAN] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
About this Structure
3ln2 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Gill A, Scanlon TC, Osipovitch DC, Madden DR, Griswold KE. Crystal structure of a charge engineered human lysozyme having enhanced bactericidal activity. PLoS One. 2011 Mar 7;6(3):e16788. PMID:21408218 doi:10.1371/journal.pone.0016788
- ↑ Pepys MB, Hawkins PN, Booth DR, Vigushin DM, Tennent GA, Soutar AK, Totty N, Nguyen O, Blake CC, Terry CJ, et al.. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature. 1993 Apr 8;362(6420):553-7. PMID:8464497 doi:http://dx.doi.org/10.1038/362553a0
Categories: Homo sapiens | Lysozyme | Gill, A. | Griswold, K E. | Scanlon, T C. | Amyloid | Amyloidosis | Antimicrobial | Bacteriolytic | Bacteriolytic enzyme | Charge engineered human lysozyme | Disease mutation | Disulfide bond | Glycosidase | Human lysozyme | Hydrolase | Protein engineering | Surface mutation