2hm1: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:
==Crystal Structure of human beta-secretase (BACE) in the presence of an inhibitor (2)==
==Crystal Structure of human beta-secretase (BACE) in the presence of an inhibitor (2)==
<StructureSection load='2hm1' size='340' side='right' caption='[[2hm1]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2hm1' size='340' side='right' caption='[[2hm1]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
Line 7: Line 8:
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BACE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BACE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hm1 OCA], [http://pdbe.org/2hm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hm1 RCSB], [http://www.ebi.ac.uk/pdbsum/2hm1 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hm1 OCA], [http://pdbe.org/2hm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hm1 RCSB], [http://www.ebi.ac.uk/pdbsum/2hm1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hm1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
Line 30: Line 31:
</div>
</div>
<div class="pdbe-citations 2hm1" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2hm1" style="background-color:#fffaf0;"></div>
==See Also==
*[[Beta secretase|Beta secretase]]
== References ==
== References ==
<references/>
<references/>

Revision as of 11:13, 18 October 2017

Crystal Structure of human beta-secretase (BACE) in the presence of an inhibitor (2)Crystal Structure of human beta-secretase (BACE) in the presence of an inhibitor (2)

Structural highlights

2hm1 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:BACE (HUMAN)
Activity:Memapsin 2, with EC number 3.4.23.46
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BACE1_HUMAN] Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We describe an optimized series of acyclic hydroxyethylamine transition state isosteres of beta-secretase that incorporates a variety of P(2) side chains that yield potent inhibitors with excellent cellular activity. A 2.2A crystal structure of compound 13 is shown.

Design of potent inhibitors of human beta-secretase. Part 2.,Freskos JN, Fobian YM, Benson TE, Moon JB, Bienkowski MJ, Brown DL, Emmons TL, Heintz R, Laborde A, McDonald JJ, Mischke BV, Molyneaux JM, Mullins PB, Bryan Prince D, Paddock DJ, Tomasselli AG, Winterrowd G Bioorg Med Chem Lett. 2007 Jan 1;17(1):78-81. Epub 2006 Oct 4. PMID:17049233[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Lin X, Koelsch G, Wu S, Downs D, Dashti A, Tang J. Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1456-60. PMID:10677483
  2. ↑ Okada H, Zhang W, Peterhoff C, Hwang JC, Nixon RA, Ryu SH, Kim TW. Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing. FASEB J. 2010 Aug;24(8):2783-94. doi: 10.1096/fj.09-146357. Epub 2010 Mar 30. PMID:20354142 doi:10.1096/fj.09-146357
  3. ↑ Freskos JN, Fobian YM, Benson TE, Moon JB, Bienkowski MJ, Brown DL, Emmons TL, Heintz R, Laborde A, McDonald JJ, Mischke BV, Molyneaux JM, Mullins PB, Bryan Prince D, Paddock DJ, Tomasselli AG, Winterrowd G. Design of potent inhibitors of human beta-secretase. Part 2. Bioorg Med Chem Lett. 2007 Jan 1;17(1):78-81. Epub 2006 Oct 4. PMID:17049233 doi:10.1016/j.bmcl.2006.09.091

2hm1, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2hm1&oldid=2790387"