1lz1

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[[Image:1lz1.png|left|200px]]
 
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{{STRUCTURE_1lz1| PDB=1lz1 | SCENE= }}
{{STRUCTURE_1lz1| PDB=1lz1 | SCENE= }}
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===REFINEMENT OF HUMAN LYSOZYME AT 1.5 ANGSTROMS RESOLUTION. ANALYSIS OF NON-BONDED AND HYDROGEN-BOND INTERACTIONS===
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===REFINEMENT OF HUMAN LYSOZYME AT 1.5 ANGSTROMS RESOLUTION. ANALYSIS OF NON-BONDED AND HYDROGEN-BOND INTERACTIONS===
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==Disease==
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[[http://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN]] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://omim.org/entry/105200 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.<ref>PMID:8464497</ref>
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==Function==
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[[http://www.uniprot.org/uniprot/LYSC_HUMAN 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==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:007334520</ref><references group="xtra"/>
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<ref group="xtra">PMID:007334520</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Artymiuk, P J.]]
[[Category: Artymiuk, P J.]]
[[Category: Blake, C C.F.]]
[[Category: Blake, C C.F.]]

Revision as of 03:06, 25 March 2013

Template:STRUCTURE 1lz1

Contents

REFINEMENT OF HUMAN LYSOZYME AT 1.5 ANGSTROMS RESOLUTION. ANALYSIS OF NON-BONDED AND HYDROGEN-BOND INTERACTIONS

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

1lz1 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Artymiuk PJ, Blake CC. Refinement of human lysozyme at 1.5 A resolution analysis of non-bonded and hydrogen-bond interactions. J Mol Biol. 1981 Nov 15;152(4):737-62. PMID:7334520
  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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