1LML

LEISHMANOLYSIN

Summary for 1LML

• Entry DOI: 10.2210/pdb1lml/pdb
• Descriptor: LEISHMANOLYSIN, ZINC ION (3 entities in total)
• Functional Keywords: leishmanolysin, metalloprotease, glycoprotein
• Biological source: Leishmania major
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: P08148
• Total number of polymer chains: 1
• Total formula weight: 51673.18

Authors

Schlagenhauf, E.,Etges, R.,Metcalf, P. (deposition date: 1997-03-13, release date: 1997-09-17, Last modification date: 2024-10-23)

Primary citation

Schlagenhauf, E.,Etges, R.,Metcalf, P.
The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63).
Structure, 6:1035-1046, 1998

PubMed Abstract: Despite their medical importance, there is little available structural information for the surface antigens of infectious protozoa. Diseases caused by the protozoan parasite Leishmania are common in many developing countries. Human infection occurs during the bite of infected sandfilies, when Leishmania promastigote cells from the insect gut enter the bloodstream. Promastigotes in the blood parasitize macrophages, often causing serious disease. Leishmanolysin is the predominant protein surface antigen of promastigotes, and is assumed to have a key role during infection. Leishmanolysin is a membrane-bound zinc proteinase, active in situ. Similar molecules exist in other trypanomastid protozoa.

PubMed: 9739094
DOI: 10.1016/S0969-2126(98)00104-X

Experimental method

X-RAY DIFFRACTION (1.86 Å)