Template:STRUCTURE 1jsf

FULL-MATRIX LEAST-SQUARES REFINEMENT OF HUMAN LYSOZYMEFULL-MATRIX LEAST-SQUARES REFINEMENT OF HUMAN LYSOZYME

Template:ABSTRACT PUBMED 9517539

DiseaseDisease

[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]

FunctionFunction

[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 StructureAbout this Structure

1jsf is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1]

  1. Harata K, Abe Y, Muraki M. Full-matrix least-squares refinement of lysozymes and analysis of anisotropic thermal motion. Proteins. 1998 Feb 15;30(3):232-43. PMID:9517539
  1. 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

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