1as4
From Proteopedia
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|PDB= 1as4 |SIZE=350|CAPTION= <scene name='initialview01'>1as4</scene>, resolution 2.1Å | |PDB= 1as4 |SIZE=350|CAPTION= <scene name='initialview01'>1as4</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ACT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= ACT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1as4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1as4 OCA], [http://www.ebi.ac.uk/pdbsum/1as4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1as4 RCSB]</span> | ||
}} | }} | ||
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==Disease== | ==Disease== | ||
| - | Known | + | Known disease associated with this structure: Alpha-1-antichymotrypsin deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107280 107280]], Cerebrovascular disease, occlusive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107280 107280]] |
==About this Structure== | ==About this Structure== | ||
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[[Category: Christianson, D W.]] | [[Category: Christianson, D W.]] | ||
[[Category: Lukacs, C M.]] | [[Category: Lukacs, C M.]] | ||
| - | [[Category: ACT]] | ||
[[Category: antichymotrypsin]] | [[Category: antichymotrypsin]] | ||
[[Category: serine protease inhibitor]] | [[Category: serine protease inhibitor]] | ||
[[Category: serpin]] | [[Category: serpin]] | ||
| - | ''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 18:46:30 2008'' |
Revision as of 15:46, 30 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ACT (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CLEAVED ANTICHYMOTRYPSIN A349R
Contents |
Overview
Expressed in a kinetically trapped folding state, a serpin couples the thermodynamic driving force of a massive beta-sheet rearrangement to the inhibition of a target protease. Hence, the serpin-protease interaction is the premier example of a "spring-loaded" protein-protein interaction. Amino acid substitutions in the hinge region of a serpin reactive loop can weaken the molecular spring, which converts the serpin from an inhibitor into a substrate. To probe the molecular basis of this conversion, we report the crystal structure of A349R antichymotrypsin in the reactive loop cleaved state at 2.1 A resolution. This amino acid substitution does not block the beta-sheet rearrangement despite the burial of R349 in the hydrophobic core of the cleaved serpin along with a salt-linked acetate ion. The inhibitory activity of this serpin variant is not obliterated; remarkably, its inhibitory properties are anion-dependent due to the creation of an anion-binding cavity in the cleaved serpin.
Disease
Known disease associated with this structure: Alpha-1-antichymotrypsin deficiency OMIM:[107280], Cerebrovascular disease, occlusive OMIM:[107280]
About this Structure
1AS4 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction., Lukacs CM, Rubin H, Christianson DW, Biochemistry. 1998 Mar 10;37(10):3297-304. PMID:9521649
Page seeded by OCA on Sun Mar 30 18:46:30 2008
