211143
constant: false
value: NaN
name: scatchard
type: Parameter

211168
constant: false
value: 0.0
name: x3
type: Parameter

211205
constant: true
value: 4.0E-4
name: k1_
type: Parameter

211217
constant: true
value: 1000000.0
name: k2
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MODEL1201140005
parameter: 211180
parameter: 211217
rule: 211278
parameter: 211205
notes: This a model from the article: Insulin receptor binding kinetics: modeling and simulation studies. Wanant S, Quon MJ. J Theor Biol. 2000 Aug 7;205(3):355-64. 10882558 , Abstract: Biological actions of insulin regulate glucose metabolism and other essential physiological functions. Binding of insulin to its cell surface receptor initiates signal transduction pathways that mediate cellular responses. Thus, it is of great interest to understand the mechanisms underlying insulin receptor binding kinetics. Interestingly, negative cooperative interactions are observed at high insulin concentrations while positive cooperativity may be present at low insulin concentrations. Clearly, insulin receptor binding kinetics cannot be simply explained by a classical bimolecular reaction. Mature insulin receptors have a dimeric structure capable of binding two molecules of insulin. The binding affinity of the receptor for the second insulin molecule is significantly lower than for the first bound insulin molecule. In addition, insulin receptor aggregation occurs in response to ligand binding and aggregation may also influence binding kinetics. In this study, we develop a mathematical model for insulin receptor binding kinetics that explicitly represents the divalent nature of the insulin receptor and incorporates receptor aggregation into the kinetic model. Model parameters are based upon published data where available. Computer simulations with our model are capable of reproducing both negative and positive cooperativity at the appropriate insulin concentrations. This model may be a useful tool for helping to understand the mechanisms underlying insulin receptor binding and the coupling of receptor binding to downstream signaling events. This model was taken from the CellML repository and automatically converted to SBML. The original model was: Wanant_Quon_2000_A The original CellML model was created by: Catherine Lloyd c.lloyd@aukland.ac.nz The University of Auckland The Bioenginee…
rule: 211241
parameter: 211143
parameter: 211192
curated: false
substance units: 163161
parameter: 211118
parameter: 211130
rule: 211290
rule: 211265
rule: 211253
parameter: 211155
compartment: 211106
area units: 802883
length unit: 802859
time units: 152087
volume units: 122997
parameter: 211168
is described by: http://identifiers.org/pubmed/10882558
name: Wanant2000_InsulinReceptorModel_A
type: SBMLModel
parameter: 211229

211180
constant: false
value: 0.0
name: x4
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211118
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value: NaN
name: time
type: Parameter

211155
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value: 0.1
name: x2
type: Parameter

211130
constant: false
value: 1000.0
name: x1
type: Parameter

211106
constant: true
size: 1.0
spatial dimensions: 3.0
type: Compartment

211192
constant: true
value: 1000000.0
name: k1
type: Parameter

211229
constant: true
value: 0.04
name: k2_
type: Parameter