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2IUE

Pactolus I-domain: Functional Switching of the Rossmann Fold

Summary for 2IUE
Entry DOI10.2210/pdb2iue/pdb
NMR InformationBMRB: 7313
DescriptorINTEGRIN BETA-2-LIKE PROTEIN (1 entity in total)
Functional Keywordsmembrane protein, cd, itc, limbs, midas, admidas, membrane, integrin, titration, cell adhesion, transmembrane
Biological sourceMUS MUSCULUS (HOUSE MOUSE)
Total number of polymer chains1
Total formula weight23433.66
Authors
Sen, M.,Legge, G.B. (deposition date: 2006-06-02, release date: 2007-06-05, Last modification date: 2024-05-15)
Primary citationSen, M.,Legge, G.B.
Pactolus I-Domain: Functional Switching of the Rossmann Fold.
Proteins, 68:626-, 2007
Cited by
PubMed Abstract: Murine Pactolus is a neutrophil-specific single chain glycoprotein that plays a role as an apoptosis marker for macrophages. The extracellular region of the protein shows strong sequence similarities to integrin beta-subunits. Critical sequence modifications differentiate its function when compared to the integrin family. We show experimentally that Pactolus I-domain does not bind divalent metal ions, indicating that ligand binding is not mediated through a metal ion-dependent adhesion site (MIDAS). NMR data was used to map secondary structure and the strand pairing within the beta-sheet to confirm an overall Rossmann fold topology. Homology modeling enhanced by the NMR data was used to determine the overall structure, with two key loop insertions/deletions (insertion 2 and SDL) that distinguish the Pactolus I-domain from the integrin alpha I-domain and beta I-domains. NMR peak exchange broadening is observed due to dimerization, correlating to the beta I-domain and beta propeller heterodimerization region within the integrin headpiece. Two unique N-linked glycosylation sites (Asn151 and Asn230) within this region disrupt dimerization and may account for why Pactolus is not found to associate with an alpha-subunit. These changes in quaternary structure, ligand binding loops, glycosylation, and metal sites illustrate how evolution has rapidly and effectively altered key aspects of the integrin beta-subunit to derive a protein of novel function on an existing protein scaffold.
PubMed: 17523188
DOI: 10.1002/PROT.21458
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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