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- PDB-1hwh: 1:1 COMPLEX OF HUMAN GROWTH HORMONE MUTANT G120R WITH ITS SOLUBLE... -

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Basic information

Entry
Database: PDB / ID: 1hwh
Title1:1 COMPLEX OF HUMAN GROWTH HORMONE MUTANT G120R WITH ITS SOLUBLE BINDING PROTEIN
Components
  • GROWTH HORMONE
  • GROWTH HORMONE BINDING PROTEIN
KeywordsCOMPLEX (HORMONE/RECEPTOR) / CYTOKINE / HORMONE / RECEPTOR / HEMATOPOIETIC / COMPLEX (HORMONE-RECEPTOR) / COMPLEX (HORMONE-RECEPTOR) complex
Function / homology
Function and homology information


growth hormone receptor activity / regulation of response to nutrient levels / growth hormone activity / growth hormone receptor complex / bone maturation / prolactin receptor binding / positive regulation of growth / taurine metabolic process / animal organ development / positive regulation of activation of Janus kinase activity ...growth hormone receptor activity / regulation of response to nutrient levels / growth hormone activity / growth hormone receptor complex / bone maturation / prolactin receptor binding / positive regulation of growth / taurine metabolic process / animal organ development / positive regulation of activation of Janus kinase activity / response to gravity / cartilage development involved in endochondral bone morphogenesis / positive regulation of multicellular organism growth / hormone metabolic process / positive regulation of glucose transmembrane transport / proline-rich region binding / positive regulation of insulin-like growth factor receptor signaling pathway / growth hormone receptor binding / response to food / growth hormone receptor signaling pathway / response to cycloheximide / Prolactin receptor signaling / cytokine binding / growth factor binding / peptide hormone binding / cell surface receptor signaling pathway via JAK-STAT / regulation of multicellular organism growth / Synthesis, secretion, and deacylation of Ghrelin / Growth hormone receptor signaling / response to glucocorticoid / positive regulation of tyrosine phosphorylation of STAT protein / cellular response to hormone stimulus / hormone-mediated signaling pathway / response to interleukin-1 / SH2 domain binding / response to nutrient levels / insulin-like growth factor receptor signaling pathway / cytokine activity / endosome lumen / positive regulation of cell differentiation / positive regulation of receptor signaling pathway via JAK-STAT / positive regulation of MAP kinase activity / growth factor activity / hormone activity / receptor internalization / cytokine-mediated signaling pathway / cytoplasmic ribonucleoprotein granule / endocytosis / cellular response to insulin stimulus / positive regulation of peptidyl-tyrosine phosphorylation / response to estradiol / protein phosphatase binding / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / external side of plasma membrane / neuronal cell body / lipid binding / protein kinase binding / cell surface / protein homodimerization activity / extracellular space / extracellular region / identical protein binding / membrane / metal ion binding / plasma membrane / cytosol
Similarity search - Function
Growth hormone-binding protein / Growth hormone receptor binding / Somatotropin / Somatotropin/prolactin / Somatotropin hormone, conserved site / Somatotropin hormone family / Somatotropin, prolactin and related hormones signature 1. / Somatotropin, prolactin and related hormones signature 2. / Long hematopoietin receptor, single chain, conserved site / Long hematopoietin receptor, single chain family signature. ...Growth hormone-binding protein / Growth hormone receptor binding / Somatotropin / Somatotropin/prolactin / Somatotropin hormone, conserved site / Somatotropin hormone family / Somatotropin, prolactin and related hormones signature 1. / Somatotropin, prolactin and related hormones signature 2. / Long hematopoietin receptor, single chain, conserved site / Long hematopoietin receptor, single chain family signature. / Growth hormone/erythropoietin receptor, ligand binding / Erythropoietin receptor, ligand binding / Growth Hormone; Chain: A; - #10 / Four-helical cytokine-like, core / Growth Hormone; Chain: A; / Fibronectin type III domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulins / Immunoglobulin-like fold / Up-down Bundle / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Somatotropin / Growth hormone receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsSundstrom, S.M. / Lundqvist, T.
CitationJournal: J.Biol.Chem. / Year: 1996
Title: Crystal structure of an antagonist mutant of human growth hormone, G120R, in complex with its receptor at 2.9 A resolution.
Authors: Sundstrom, M. / Lundqvist, T. / Rodin, J. / Giebel, L.B. / Milligan, D. / Norstedt, G.
History
DepositionNov 13, 1996Processing site: BNL
Revision 1.0Nov 19, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GROWTH HORMONE
B: GROWTH HORMONE BINDING PROTEIN


Theoretical massNumber of molelcules
Total (without water)49,5342
Polymers49,5342
Non-polymers00
Water00
1
A: GROWTH HORMONE
B: GROWTH HORMONE BINDING PROTEIN

A: GROWTH HORMONE
B: GROWTH HORMONE BINDING PROTEIN


Theoretical massNumber of molelcules
Total (without water)99,0684
Polymers99,0684
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_555y,x,-z1
Unit cell
Length a, b, c (Å)67.780, 67.780, 229.240
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein GROWTH HORMONE


Mass: 22252.135 Da / Num. of mol.: 1 / Mutation: G120R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P01241
#2: Protein GROWTH HORMONE BINDING PROTEIN


Mass: 27281.641 Da / Num. of mol.: 1 / Fragment: EXTRACELLULAR DOMAIN
Source method: isolated from a genetically manipulated source
Details: ONE HORMONE WITH ONE RECEPTOR MOLECULE / Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P10912

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 2

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Sample preparation

CrystalDensity Matthews: 2.66 Å3/Da / Density % sol: 55 %
Crystal growpH: 6.75
Details: THE PROTEIN COMPLEX WAS CRYSTALLISED FROM 1.6 M LISO4 AND 50 MM BIS TRIS AT PH 6.75
Crystal grow
*PLUS
Temperature: 18 ℃ / pH: 6.25 / Method: vapor diffusion
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
146 %(v/v)sat1reservoirLiSO4
22 %PEG5001reservoir
310 mg/mlprotein1drop

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Data collection

DiffractionMean temperature: 293 K
Diffraction sourceWavelength: 1.5418
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 1, 1995
RadiationMonochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionHighest resolution: 2.9 Å / Num. obs: 11596 / % possible obs: 91.8 % / Observed criterion σ(I): 2 / Redundancy: 4.1 % / Rsym value: 0.099 / Net I/σ(I): 11
Reflection shellResolution: 2.9→3 Å / Rsym value: 0.296
Reflection
*PLUS
Lowest resolution: 20 Å / Rmerge(I) obs: 0.099
Reflection shell
*PLUS
% possible obs: 77.1 % / Rmerge(I) obs: 0.296

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
CCP4data reduction
X-PLOR3.1model building
X-PLOR3.1refinement
CCP4data scaling
X-PLOR3.1phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.9→20 Å / Cross valid method: THROUGHOUT / σ(F): 2
RfactorNum. reflection% reflectionSelection details
Rfree0.317 580 5 %RANDOM
Rwork0.215 ---
obs0.215 11596 91.8 %-
Displacement parametersBiso mean: 27.7 Å2
Refinement stepCycle: LAST / Resolution: 2.9→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3701 0 0 0 3701
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.013
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.94
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
LS refinement shellResolution: 2.9→3 Å / Total num. of bins used: 6 /
Rfactor% reflection
Rwork0.296 -
obs-77.1 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PARHCSDX.PROTOPHCSDX.PRO
X-RAY DIFFRACTION2

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