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The multiple roles of histidine in protein interactions.

ABSTRACT: BACKGROUND:Among the 20 natural amino acids histidine is the most active and versatile member that plays the multiple roles in protein interactions, often the key residue in enzyme catalytic reactions. A theoretical and comprehensive study on the structural features and interaction properties of histidine is certainly helpful. RESULTS:Four interaction types of histidine are quantitatively calculated, including: (1) Cation-? interactions, in which the histidine acts as the aromatic ?-motif in neutral form (His), or plays the cation role in protonated form (His+); (2) ?-? stacking interactions between histidine and other aromatic amino acids; (3) Hydrogen-? interactions between histidine and other aromatic amino acids; (4) Coordinate interactions between histidine and metallic cations. The energies of ?-? stacking interactions and hydrogen-? interactions are calculated using CCSD/6-31+G(d,p). The energies of cation-? interactions and coordinate interactions are calculated using B3LYP/6-31+G(d,p) method and adjusted by empirical method for dispersion energy. CONCLUSIONS:The coordinate interactions between histidine and metallic cations are the strongest one acting in broad range, followed by the cation-?, hydrogen-?, and ?-? stacking interactions. When the histidine is in neutral form, the cation-? interactions are attractive; when it is protonated (His+), the interactions turn to repulsive. The two protonation forms (and pKa values) of histidine are reversibly switched by the attractive and repulsive cation-? interactions. In proteins the ?-? stacking interaction between neutral histidine and aromatic amino acids (Phe, Tyr, Trp) are in the range from -3.0 to -4.0 kcal/mol, significantly larger than the van der Waals energies.

SUBMITTER: Liao SM

PROVIDER: S-EPMC3599372 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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The multiple roles of histidine in protein interactions.

Liao Si-Ming SM Du Qi-Shi QS Meng Jian-Zong JZ Pang Zong-Wen ZW Huang Ri-Bo RB

Chemistry Central journal 20130301 1

<h4>Background</h4>Among the 20 natural amino acids histidine is the most active and versatile member that plays the multiple roles in protein interactions, often the key residue in enzyme catalytic reactions. A theoretical and comprehensive study on the structural features and interaction properties of histidine is certainly helpful.<h4>Results</h4>Four interaction types of histidine are quantitatively calculated, including: (1) Cation-π interactions, in which the histidine acts as the aromatic ...[more]

PMID: 23452343

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Project description:RationaleDefects in the morphogenesis of the fourth pharyngeal arch arteries (PAAs) give rise to lethal birth defects. Understanding genes and mechanisms regulating PAA formation will provide important insights into the etiology and treatments for congenital heart disease.ObjectiveCell-ECM (extracellular matrix) interactions play essential roles in the morphogenesis of PAAs and their derivatives, the aortic arch artery and its major branches; however, their specific functions are not well-understood. Previously, we demonstrated that integrin α5β1 and Fn1 (fibronectin) expressed in the Isl1 lineages regulate PAA formation. The objective of the current studies was to investigate cellular mechanisms by which integrin α5β1 and Fn1 regulate aortic arch artery morphogenesis.Methods and resultsUsing temporal lineage tracing, whole-mount confocal imaging, and quantitative analysis of the second heart field (SHF) and endothelial cell (EC) dynamics, we show that the majority of PAA EC progenitors arise by E7.5 in the SHF and contribute to pharyngeal arch endothelium between E7.5 and E9.5. Consequently, SHF-derived ECs in the pharyngeal arches form a plexus of small blood vessels, which remodels into the PAAs by 35 somites. The remodeling of the vascular plexus is orchestrated by signals dependent on the pharyngeal ECM microenvironment, extrinsic to the endothelium. Conditional ablation of integrin α5β1 or Fn1 in the Isl1 lineages showed that signaling by the ECM regulates aortic arch artery morphogenesis at multiple steps: (1) accumulation of SHF-derived ECs in the pharyngeal arches, (2) remodeling of the EC plexus in the fourth arches into the PAAs, and (3) differentiation of neural crest-derived cells adjacent to the PAA endothelium into vascular smooth muscle cells.ConclusionsPAA formation is a multistep process entailing dynamic contribution of SHF-derived ECs to pharyngeal arches, the remodeling of endothelial plexus into the PAAs, and the remodeling of the PAAs into the aortic arch artery and its major branches. Cell-ECM interactions regulated by integrin α5β1 and Fn1 play essential roles at each of these developmental stages.

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The multiple roles of histidine in protein interactions.

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The multiple roles of histidine in protein interactions.

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