Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.24.55 (
PTR
)
433
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Zinc modulates the biological function of
histidine-rich glycoprotein
(
HRG
) through binding to its His-rich region (HRR). The Zn
2+
-binding properties of a 35 amino-acid biologically-active peptide mimic of the HRR, HRGP330, were investigated using dissociative mass spectrometry approaches in addition to travelling-wave ion mobility mass spectrometry (TWIM-MS). Native mass spectrometry confirmed zinc binding to HRGP330; however, broadening of the
1
H NMR resonances upon addition of Zn
2+
ions precluded the attainment of structural information. A complementary approach employing TWIM-MS indicated that HRGP330 has a more compact structure in the presence of Zn
2+
ions. Top-down MS/MS data supported a metal-binding-induced conformational change, as fewer fragments were observed for Zn
2+
-bound HRGP330. Zn
2+
-bound fragments of both N-terminal and C-terminal ends of the peptide were identified from collision-induced dissociation (CID) and electron transfer dissociation/proton transfer reaction (ETD/
PTR
) experiments, suggesting that multiple binding sites exist within this region of
HRG
. The combination of mass spectrometry and NMR approaches provides new insight into the highly dynamic interaction between zinc and this His-rich peptide.
...
PMID:Native electrospray mass spectrometry approaches to probe the interaction between zinc and an anti-angiogenic peptide from histidine-rich glycoprotein. 2987 14
