1iz2

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|PDB= 1iz2 |SIZE=350|CAPTION= <scene name='initialview01'>1iz2</scene>, resolution 2.20&Aring;
|PDB= 1iz2 |SIZE=350|CAPTION= <scene name='initialview01'>1iz2</scene>, resolution 2.20&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SUM:2-[3,4-DIHYDROXY-2-HYDROXYMETHYL-5-(2-HYDROXY-NONYL)-TETRAHYDRO-FURAN-2-YLOXY]-6-HYDROXYMETHYL-TETRA HYDRO-PYRAN-3,4,5-TRIOL'>SUM</scene>
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|LIGAND= <scene name='pdbligand=SUM:2-[3,4-DIHYDROXY-2-HYDROXYMETHYL-5-(2-HYDROXY-NONYL)-TETRAHYDRO-FURAN-2-YLOXY]-6-HYDROXYMETHYL-TETRA+HYDRO-PYRAN-3,4,5-TRIOL'>SUM</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iz2 OCA], [http://www.ebi.ac.uk/pdbsum/1iz2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iz2 RCSB]</span>
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==Overview==
==Overview==
Conformational transition is fundamental to the mechanism of functional regulation in proteins, and serpins (serine protease inhibitors) can provide insight into this process. Serpins are metastable in their native forms, and they ordinarily undergo conformational transition to a stable state only when they form a tight complex with target proteases. The metastable native form is thus considered to be a kinetically trapped folding intermediate. We sought to understand the nature of the serpin kinetic trap as a step toward discovering how conformational transition is regulated. We found that mutations of the B/C beta-barrel of native alpha(1)-antitrypsin, a prototypical serpin, allowed conversion of the molecule into a more stable state. A 2.2 A resolution crystal structure of the stable form (PDB code, ) showed that the reactive site loop is inserted into an A beta-sheet, as in the latent plasminogen activator inhibitor-1. Mutational analyses suggest strongly that interactions not found in the final stable form cause the kinetic trap in serpin protein folding.
Conformational transition is fundamental to the mechanism of functional regulation in proteins, and serpins (serine protease inhibitors) can provide insight into this process. Serpins are metastable in their native forms, and they ordinarily undergo conformational transition to a stable state only when they form a tight complex with target proteases. The metastable native form is thus considered to be a kinetically trapped folding intermediate. We sought to understand the nature of the serpin kinetic trap as a step toward discovering how conformational transition is regulated. We found that mutations of the B/C beta-barrel of native alpha(1)-antitrypsin, a prototypical serpin, allowed conversion of the molecule into a more stable state. A 2.2 A resolution crystal structure of the stable form (PDB code, ) showed that the reactive site loop is inserted into an A beta-sheet, as in the latent plasminogen activator inhibitor-1. Mutational analyses suggest strongly that interactions not found in the final stable form cause the kinetic trap in serpin protein folding.
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==Disease==
 
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Known diseases associated with this structure: Emphysema OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107400 107400]], Emphysema-cirrhosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107400 107400]], Hemorrhagic diathesis due to antithrombin Pittsburgh OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107400 107400]], Pulmonary disease, chronic obstructive, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107400 107400]]
 
==About this Structure==
==About this Structure==
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[[Category: Woo, M S.]]
[[Category: Woo, M S.]]
[[Category: Yu, M H.]]
[[Category: Yu, M H.]]
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[[Category: SUM]]
 
[[Category: antitrypsin]]
[[Category: antitrypsin]]
[[Category: folding]]
[[Category: folding]]
[[Category: serpin]]
[[Category: serpin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:56:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:26:42 2008''

Revision as of 18:26, 30 March 2008

Image:1iz2.gif


PDB ID 1iz2

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Interactions causing the kinetic trap in serpin protein folding


Overview

Conformational transition is fundamental to the mechanism of functional regulation in proteins, and serpins (serine protease inhibitors) can provide insight into this process. Serpins are metastable in their native forms, and they ordinarily undergo conformational transition to a stable state only when they form a tight complex with target proteases. The metastable native form is thus considered to be a kinetically trapped folding intermediate. We sought to understand the nature of the serpin kinetic trap as a step toward discovering how conformational transition is regulated. We found that mutations of the B/C beta-barrel of native alpha(1)-antitrypsin, a prototypical serpin, allowed conversion of the molecule into a more stable state. A 2.2 A resolution crystal structure of the stable form (PDB code, ) showed that the reactive site loop is inserted into an A beta-sheet, as in the latent plasminogen activator inhibitor-1. Mutational analyses suggest strongly that interactions not found in the final stable form cause the kinetic trap in serpin protein folding.

About this Structure

1IZ2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Interactions causing the kinetic trap in serpin protein folding., Im H, Woo MS, Hwang KY, Yu MH, J Biol Chem. 2002 Nov 29;277(48):46347-54. Epub 2002 Sep 18. PMID:12244055

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