1xn3: Difference between revisions

Revision as of 12:56, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1xn3.png

Template:STRUCTURE 1xn3

Crystal structure of Beta-secretase bound to a long inhibitor with additional upstream residues.Crystal structure of Beta-secretase bound to a long inhibitor with additional upstream residues.

Template:ABSTRACT PUBMED 15628850

About this StructureAbout this Structure

1XN3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural locations and functional roles of new subsites S5, S6, and S7 in memapsin 2 (beta-secretase)., Turner RT 3rd, Hong L, Koelsch G, Ghosh AK, Tang J, Biochemistry. 2005 Jan 11;44(1):105-12. PMID:15628850

Page seeded by OCA on Mon Jul 28 12:56:14 2008

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

OCA

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 {{STRUCTURE_1xn3|  PDB=1xn3  |  SCENE=  }}
-'''Crystal structure of Beta-secretase bound to a long inhibitor with additional upstream residues.'''
+===Crystal structure of Beta-secretase bound to a long inhibitor with additional upstream residues.===
-==Overview==
+<!--
-Memapsin 2 (beta-secretase) is the membrane-anchored aspartic protease that initiates the cleavage of beta-amyloid precursor protein (APP), leading to the production of amyloid-beta (Abeta), a major factor in the pathogenesis of Alzheimer's disease. The active site of memapsin 2 has been shown, with kinetic data and crystal structures, to bind to eight substrate residues (P(4)-P(4)'). We describe here that the addition of three substrate residues from P(7) to P(5) strongly influences the hydrolytic activity by memapsin 2 and these subsites prefer hydrophobic residues, especially tryptophan. A crystal structure of memapsin 2 complexed with a statine-based inhibitor spanning P(10)-P(4)' revealed the binding positions of P(5)-P(7) residues. Kinetic studies revealed that the addition of these substrate residues contributes to the decrease in K(m) and increase in k(cat) values, suggesting that these residues contribute to both substrate recognition and transition-state binding. The crystal structure of a new inhibitor, OM03-4 (K(i) = 0.03 nM), bound to memapsin 2 revealed the interaction of a tryptophan with the S(6) subsite of the protease.
+The line below this paragraph, {{ABSTRACT_PUBMED_15628850}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15628850 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15628850}}
 ==About this Structure==
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 [[Category: Drug design]]
 [[Category: Memapsin2]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:14:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:56:14 2008''