From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
Line 1: |
Line 1: |
- | [[Image:1db2.jpg|left|200px]] | + | {{Seed}} |
| + | [[Image:1db2.png|left|200px]] |
| | | |
| <!-- | | <!-- |
Line 9: |
Line 10: |
| {{STRUCTURE_1db2| PDB=1db2 | SCENE= }} | | {{STRUCTURE_1db2| PDB=1db2 | SCENE= }} |
| | | |
- | '''CRYSTAL STRUCTURE OF NATIVE PLASMINOGEN ACTIVATOR INHIBITOR-1'''
| + | ===CRYSTAL STRUCTURE OF NATIVE PLASMINOGEN ACTIVATOR INHIBITOR-1=== |
| | | |
| | | |
- | ==Overview==
| + | <!-- |
- | The crystal structure of a constitutively active multiple site mutant of plasminogen activator inhibitor 1 (PAI-1) was determined and refined at a resolution of 2.7 A.The present structure comprises a dimer of two crystallographically independent PAI-1 molecules that pack by association of the residues P6 to P3 of the reactive centre loop of one molecule (A) with the edge of the main beta-sheet A of the other molecule (B).Thus, the reactive centre loop is ordered for molecule A by crystal packing forces, while for molecule B it is unconstrained by crystal packing contacts and is disordered.The overall structure of active PAI-1 is similar to the structures of other active inhibitory serpins exhibiting as the major secondary structural feature a five-stranded beta-sheet A and an intact proteinase-binding loop protruding from the one end of the elongated molecule. No preinsertion of the reactive centre loop is observed in this structure.A comparison of the present structure with the previously determined crystal structures of PAI-1 in its alternative conformations reveals that, upon cleavage of an intact form of PAI-1 or formation of latent PAI-1, the well-characterised rearrangements of the serpin secondary structural elements are accompanied by dramatic and partly unexpected conformational changes of helical and loop structures proximal to beta-sheet A.The present structure explains the stabilising effects of the mutated residues, reveals the structural cause for the observed spectroscopic differences between active and latent PAI-1, and provides new insights into possible mechanisms of stabilisation by its natural binding partner, vitronectin. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10731421}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 10731421 is the PubMed ID number. |
| + | --> |
| + | {{ABSTRACT_PUBMED_10731421}} |
| | | |
| ==About this Structure== | | ==About this Structure== |
Line 30: |
Line 34: |
| [[Category: Hydrolase inhibitor]] | | [[Category: Hydrolase inhibitor]] |
| [[Category: Native serpin]] | | [[Category: Native serpin]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:39:01 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:46:08 2008'' |
Revision as of 19:46, 30 June 2008
Template:STRUCTURE 1db2
CRYSTAL STRUCTURE OF NATIVE PLASMINOGEN ACTIVATOR INHIBITOR-1
Template:ABSTRACT PUBMED 10731421
About this Structure
1DB2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation., Nar H, Bauer M, Stassen JM, Lang D, Gils A, Declerck PJ, J Mol Biol. 2000 Mar 31;297(3):683-95. PMID:10731421
Page seeded by OCA on Mon Jun 30 22:46:08 2008