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- PDB-1tiu: TITIN, IG REPEAT 27, NMR, 24 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1tiu
TitleTITIN, IG REPEAT 27, NMR, 24 STRUCTURES
ComponentsTITIN, I27
KeywordsIMMUNOGLOBULIN-LIKE DOMAIN / MUSCLE PROTEIN
Function / homology
Function and homology information


sarcomerogenesis / titin-telethonin complex / structural molecule activity conferring elasticity / skeletal muscle myosin thick filament assembly / telethonin binding / detection of muscle stretch / protein kinase A signaling / muscle alpha-actinin binding / cardiac myofibril assembly / mitotic chromosome condensation ...sarcomerogenesis / titin-telethonin complex / structural molecule activity conferring elasticity / skeletal muscle myosin thick filament assembly / telethonin binding / detection of muscle stretch / protein kinase A signaling / muscle alpha-actinin binding / cardiac myofibril assembly / mitotic chromosome condensation / cardiac muscle hypertrophy / cardiac muscle tissue morphogenesis / actinin binding / Striated Muscle Contraction / muscle filament sliding / protein kinase regulator activity / M band / I band / cardiac muscle cell development / structural constituent of muscle / sarcomere organization / striated muscle thin filament / skeletal muscle thin filament assembly / skeletal muscle contraction / striated muscle contraction / cardiac muscle contraction / muscle contraction / condensed nuclear chromosome / positive regulation of protein secretion / Z disc / response to calcium ion / actin filament binding / Platelet degranulation / protease binding / protein tyrosine kinase activity / eukaryotic translation initiation factor 2alpha kinase activity / 3-phosphoinositide-dependent protein kinase activity / DNA-dependent protein kinase activity / ribosomal protein S6 kinase activity / histone H3S10 kinase activity / histone H2AXS139 kinase activity / histone H3S28 kinase activity / histone H4S1 kinase activity / histone H2BS14 kinase activity / histone H3T3 kinase activity / histone H2AS121 kinase activity / Rho-dependent protein serine/threonine kinase activity / histone H2BS36 kinase activity / histone H3S57 kinase activity / histone H2AT120 kinase activity / AMP-activated protein kinase activity / histone H2AS1 kinase activity / histone H3T6 kinase activity / histone H3T11 kinase activity / histone H3T45 kinase activity / non-specific serine/threonine protein kinase / calmodulin binding / protein serine kinase activity / protein serine/threonine kinase activity / calcium ion binding / positive regulation of gene expression / protein kinase binding / enzyme binding / protein homodimerization activity / extracellular exosome / extracellular region / ATP binding / identical protein binding / cytosol
Similarity search - Function
PPAK motif / PPAK motif / Titin, Z repeat / Titin Z / MyBP-C, tri-helix bundle domain / Tri-helix bundle domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain ...PPAK motif / PPAK motif / Titin, Z repeat / Titin Z / MyBP-C, tri-helix bundle domain / Tri-helix bundle domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin V-set domain / Tyrosine-protein kinase, active site / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Protein kinase domain / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Immunoglobulins / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsImprota, S. / Politou, A.S. / Pastore, A.
Citation
Journal: Structure / Year: 1996
Title: Immunoglobulin-like modules from titin I-band: extensible components of muscle elasticity.
Authors: Improta, S. / Politou, A.S. / Pastore, A.
#1: Journal: Structure / Year: 1995
Title: Tertiary Structure of an Immunoglobulin-Like Domain from the Giant Muscle Protein Titin: A New Member of the I Set
Authors: Pfuhl, M. / Pastore, A.
#2: Journal: Science / Year: 1995
Title: Titins: Giant Proteins in Charge of Muscle Ultrastructure and Elasticity
Authors: Labeit, S. / Kolmerer, B.
History
DepositionFeb 2, 1996Processing site: BNL
Revision 1.0Jul 11, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure viewerMolecule:
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Assembly

Deposited unit
A: TITIN, I27


Theoretical massNumber of molelcules
Total (without water)10,9281
Polymers10,9281
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)24 / -
Representative

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Components

#1: Protein TITIN, I27 / CONNECTIN / I27 / TITIN IG REPEAT 27


Mass: 10928.426 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: SOLUTION STRUCTURE, T=308K, PH 4.5, 10MM ACETATE BUFFER
Source: (gene. exp.) Homo sapiens (human) / Tissue: MUSCLE / Cell line: 293 / Gene: TITIN GENE / Organ: HEART / Organelle: SARCOMERE / Plasmid: PET8C / Species (production host): Escherichia coli / Gene (production host): TITIN GENE / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q10466, UniProt: Q8WZ42*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR softwareName: X-PLOR (EXTENDED VERSION) / Version: VERSION) / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 24

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