1JRR

HUMAN PLASMINOGEN ACTIVATOR INHIBITOR-2.[LOOP (66-98) DELETIONMUTANT] COMPLEXED WITH PEPTIDE MIMIckING THE REACTIVE CENTER LOOP

Summary for 1JRR

• Entry DOI: 10.2210/pdb1jrr/pdb
• Related: 1BY7
• Descriptor: PLASMINOGEN ACTIVATOR INHIBITOR-2, BETA-MERCAPTOETHANOL, ... (4 entities in total)
• Functional Keywords: serpin, peptide binding, peptide binding protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: P05120 P05120
• Total number of polymer chains: 2
• Total formula weight: 44428.59

Authors

Jankova, L.,Harrop, S.J.,Saunders, D.N.,Andrews, J.L.,Bertram, K.C.,Gould, A.R.,Baker, M.S.,Curmi, P.M.G. (deposition date: 2001-08-15, release date: 2001-09-26, Last modification date: 2025-03-26)

Primary citation

JANKOVA, L.,HARROP, S.J.,SAUNDERS, D.N.,ANDREWS, J.L.,BERTRAM, K.C.,GOULD, A.R.,BAKER, M.S.,CURMI, P.M.G.
CRYSTAL STRUCTURE OF THE COMPLEX OF PLASMINOGEN ACTIVATOR INHIBITOR 2 WITH A PEPTIDE MIMICKING THE REACTIVE CENTER LOOP
J.Biol.Chem., 276:43374-43382, 2001

PubMed Abstract: The structure of the serpin, plasminogen activator inhibitor type-2 (PAI-2), in a complex with a peptide mimicking its reactive center loop (RCL) has been determined at 1.6-A resolution. The structure shows the relaxed state serpin structure with a prominent six-stranded beta-sheet. Clear electron density is seen for all residues in the peptide. The P1 residue of the peptide binds to a well defined pocket at the base of PAI-2 that may be important in determining the specificity of protease inhibition. The stressed-to-relaxed state (S --> R) transition in PAI-2 can be modeled as the relative motion between a quasirigid core domain and a smaller segment comprising helix hF and beta-strands s1A, s2A, and s3A. A comparison of the Ramachandran plots of the stressed and relaxed state PAI-2 structures reveals the location of several hinge regions connecting these two domains. The hinge regions cluster in three locations on the structure, ensuring a cooperative S --> R transition. We hypothesize that the hinge formed by the conserved Gly(206) on beta-strand s3A in the breach region of PAI-2 effects the S --> R transition by altering its backbone torsion angles. This torsional change is due to the binding of the P14 threonine of the RCL to the open breach region of PAI-2.

PubMed: 11546761
DOI: 10.1074/jbc.M103021200

Experimental method

X-RAY DIFFRACTION (1.6 Å)