1sgz
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Memapsin_2 Memapsin 2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.46 3.4.23.46] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Memapsin_2 Memapsin 2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.46 3.4.23.46] </span> |
|GENE= BACE, BACE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= BACE, BACE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1fkn|1FKN]], [[1m4h|1M4H]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sgz OCA], [http://www.ebi.ac.uk/pdbsum/1sgz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sgz RCSB]</span> | ||
}} | }} | ||
| Line 34: | Line 37: | ||
[[Category: protease flap]] | [[Category: protease flap]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:41:57 2008'' |
Revision as of 20:41, 30 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | BACE, BACE1 (Homo sapiens) | ||||||
| Activity: | Memapsin 2, with EC number 3.4.23.46 | ||||||
| Related: | 1FKN, 1M4H
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Unbound Beta-Secretase Catalytic Domain.
Overview
The three-dimensional structure of unbound human memapsin 2 (beta-secretase) protease domain determined at 2.0-A resolution has revealed a new position of the flap region, which appears to be locked in an "open" position. While the structure outside of the flap is essentially the same as the structure of memapsin 2 bound to an inhibitor, the flap positions are 4.5 A different at the tips. The open position of the flap in the current structure is stabilized by two newly formed intraflap hydrogen bonds and anchored by a new hydrogen bond involving the side chain of Tyr 71 (Tyr 75 in pepsin numbering) in a novel orientation. In molecular modeling experiments, the opening of the flap, 6.5 A at the narrowest point, permits entrance of substrates into the cleft. The narrowest point of the opening may function to discriminate among substrates based on sequence and shape. The observed flap opening may also serve as a model for the flap movement in the catalytic mechanism of eukaryotic aspartic proteases and provide insight for the side-chain selection in the design of memapsin 2 inhibitors.
About this Structure
1SGZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Flap position of free memapsin 2 (beta-secretase), a model for flap opening in aspartic protease catalysis., Hong L, Tang J, Biochemistry. 2004 Apr 27;43(16):4689-95. PMID:15096037
Page seeded by OCA on Sun Mar 30 23:41:57 2008
Categories: Homo sapiens | Memapsin 2 | Single protein | Hong, L. | Tang, J. | Alzheimer's disease | Asp2 | Aspartic protease | Bace | Beta-secretase | Drug design | Memapsin | Protease flap
