View source for 1di5

{{STRUCTURE_1di5|  PDB=1di5  |  SCENE=  }} 
===ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME===
{{ABSTRACT_PUBMED_10913274}}

==Disease==
[[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> 

==Function==
[[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==
[[1di5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DI5 OCA]. 

==See Also==
*[[Hen Egg-White (HEW) Lysozyme|Hen Egg-White (HEW) Lysozyme]]

==Reference==
<ref group="xtra">PMID:010913274</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Lysozyme]]
[[Category: Takano, K.]]
[[Category: Yamagata, Y.]]
[[Category: Yutani, K.]]
[[Category: Hydrolase]]
[[Category: Mutant]]
[[Category: Stability]]
[[Category: Turn]]