1yth

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[[Image:1yth.jpg|left|200px]]
[[Image:1yth.jpg|left|200px]]
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{{Structure
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|PDB= 1yth |SIZE=350|CAPTION= <scene name='initialview01'>1yth</scene>, resolution 2.2&Aring;
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The line below this paragraph, containing "STRUCTURE_1yth", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= STRAIN SF-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1yth| PDB=1yth | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yth OCA], [http://www.ebi.ac.uk/pdbsum/1yth PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yth RCSB]</span>
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'''SIV PROTEASE CRYSTALLIZED WITH PEPTIDE PRODUCT'''
'''SIV PROTEASE CRYSTALLIZED WITH PEPTIDE PRODUCT'''
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[[Category: Rose, R B.]]
[[Category: Rose, R B.]]
[[Category: Stroud, R M.]]
[[Category: Stroud, R M.]]
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[[Category: aspartyl protease]]
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[[Category: Aspartyl protease]]
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[[Category: complex (hydrolase/peptide,) aid]]
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[[Category: Endonuclease]]
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[[Category: endonuclease]]
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[[Category: Hydrolase]]
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[[Category: hydrolase]]
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[[Category: Polyprotein]]
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[[Category: polyprotein]]
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[[Category: Rna-directed dna polymerase]]
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[[Category: rna-directed dna polymerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:46:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:21:52 2008''
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Revision as of 13:46, 3 May 2008

Image:1yth.jpg

Template:STRUCTURE 1yth

SIV PROTEASE CRYSTALLIZED WITH PEPTIDE PRODUCT


Overview

Strain is eliminated as a factor in hydrolysis of the scissile peptide bond by human immunodeficiency virus (HIV)-1 and simian immunodeficiency virus (SIV), based on the first eight complexes of products of hydrolysis with the enzymes. The carboxyl group generated at the scissile bond interacts with both catalytic aspartic acids. The structures directly suggest the interactions of the gemdiol intermediate with the active site. Based on the structures, the nucleophilic water is displaced stereospecifically by substrate binding toward one catalytic aspartic acid, while the scissile carbonyl becomes hydrogen bonded to the other catalytic aspartic acid in position for hydrolysis. Crystal structures for two N-terminal (P) products and two C-terminal (Q) products provide unambiguous density for the ligands at 2.2-2.6 A resolution and 17-21% R factors. The N-terminal product, Ac-S-L-N-F/, overlaps closely with the N-terminal sequences of peptidomimetic inhibitors bound to the protease. Comparison of the two C-terminal products, /F-L-E-K and /F(NO2)-E-A-Nle-S, indicates that the P2' residue is highly constrained, while the positioning of the P1' and P3' residues are sequence dependent.

About this Structure

1YTH is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Three-dimensional structures of HIV-1 and SIV protease product complexes., Rose RB, Craik CS, Douglas NL, Stroud RM, Biochemistry. 1996 Oct 1;35(39):12933-44. PMID:8841139 Page seeded by OCA on Sat May 3 16:46:09 2008

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OCA

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