4l3t
From Proteopedia
(Difference between revisions)
m (Protected "4l3t" [edit=sysop:move=sysop]) |
|||
Line 1: | Line 1: | ||
- | + | {{STRUCTURE_4l3t| PDB=4l3t | SCENE= }} | |
+ | ===Crystal Structure of Substrate-free Human Presequence Protease=== | ||
- | + | ==Function== | |
+ | [[http://www.uniprot.org/uniprot/PREP_HUMAN PREP_HUMAN]] ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Able to degrade amyloid beta A4 (APP) protein when it accumulates in mitochondrion, suggesting a link with Alzheimer disease. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference.<ref>PMID:16849325</ref> | ||
- | + | ==About this Structure== | |
+ | [[4l3t]] is a 2 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=4L3T OCA]. | ||
- | + | ==Reference== | |
+ | <references group="xtra"/><references/> | ||
+ | [[Category: Homo sapiens]] | ||
+ | [[Category: King, J V.]] | ||
+ | [[Category: Liang, W G.]] | ||
+ | [[Category: Tang, W J.]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Mitochondrial matrix]] | ||
+ | [[Category: Zinc metalloendoprotease]] |
Revision as of 14:20, 3 July 2013
Contents |
Crystal Structure of Substrate-free Human Presequence Protease
Function
[PREP_HUMAN] ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Able to degrade amyloid beta A4 (APP) protein when it accumulates in mitochondrion, suggesting a link with Alzheimer disease. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference.[1]
About this Structure
4l3t is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- ↑ Falkevall A, Alikhani N, Bhushan S, Pavlov PF, Busch K, Johnson KA, Eneqvist T, Tjernberg L, Ankarcrona M, Glaser E. Degradation of the amyloid beta-protein by the novel mitochondrial peptidasome, PreP. J Biol Chem. 2006 Sep 29;281(39):29096-104. Epub 2006 Jul 18. PMID:16849325 doi:M602532200