What question did this study set out to answer?

Determine the complete primary structure, domain architecture, and pH-dependent conformational behavior of rabbit plasma histidine-proline-rich glycoprotein (HPRG).

January 1, 1996Biochemistry

Domain Structure and Conformation of Histidine−Proline-Rich Glycoprotein,

View Full Paper

Ask AI

Bookmark

Determine the complete primary structure, domain architecture, and pH-dependent conformational behavior of rabbit plasma histidine-proline-rich glycoprotein (HPRG).
Determined the primary sequence of rabbit plasma HPRG using cDNA and peptide sequencing.
Isolated and characterized domain fragments using limited plasmin proteolysis, dithiothreitol reduction, and far-UV circular dichroism spectroscopy.
Evaluated pH-induced conformational changes using solvent perturbation and second-derivative UV spectroscopy.
Revealed a modular structure consisting of two N-terminal cystatin-like modules (beta-sheet and alpha-helix), a central domain with 15 pentapeptide repeats (polyproline-II helix), and a C-terminal region (random coil).
Demonstrated that the central domain contains 34 histidine residues with an apparent pKa of 7.0 and an isoelectric point of 7.15, mediating pH-sensitive heparin binding between pH 7.0 and 7.4.
Identified a conformational transition with a midpoint at pH 6.0 driven by electrostatic repulsion among protonated histidines and transmitted to the rest of the protein via a disulfide bond.

Discussion

No takes yet. Share an insight, caveat, or question.

Implication

Structural analysis reveals modular domains and pH-sensitive conformational shifts in rabbit histidine-proline-rich glycoprotein, suggesting a mechanism for regulated multivalent ligand binding.

Cite This Study

Borza et al. (1996) studied this question.

synapsesocial.com/papers/6a775133576efb0ddaf74116 https://doi.org/10.1021/bi952061t

View Full Paper

Ask AI

Bookmark

Implication

Structural analysis reveals modular domains and pH-sensitive conformational shifts in rabbit histidine-proline-rich glycoprotein, suggesting a mechanism for regulated multivalent ligand binding.

Domain Structure and Conformation of Histidine−Proline-Rich Glycoprotein,

Key Points

Discussion

Implication

Cite This Study

Domain Structure and Conformation of Histidine−Proline-Rich Glycoprotein,

Key Points

Discussion

Implication

Cite This Study

Also Consider

Also Consider