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- PDB-1apj: NMR STUDY OF THE TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-... -

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Entry
Database: PDB / ID: 1apj
TitleNMR STUDY OF THE TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-LIKE DOMAIN (TB MODULE/8-CYS DOMAIN), NMR, 21 STRUCTURES
ComponentsFIBRILLIN
KeywordsEXTRACELLULAR MATRIX / FIBRILLIN FRAGMENT / MICROFIBRIL / TB MODULE / MARFAN SYNDROME / CONNECTIVE TISSUE / NOVEL FOLD
Function / homology
Function and homology information


post-embryonic eye morphogenesis / extracellular matrix constituent conferring elasticity / sequestering of BMP in extracellular matrix / sequestering of TGFbeta in extracellular matrix / microfibril / embryonic eye morphogenesis / negative regulation of osteoclast development / metanephros development / camera-type eye development / Elastic fibre formation ...post-embryonic eye morphogenesis / extracellular matrix constituent conferring elasticity / sequestering of BMP in extracellular matrix / sequestering of TGFbeta in extracellular matrix / microfibril / embryonic eye morphogenesis / negative regulation of osteoclast development / metanephros development / camera-type eye development / Elastic fibre formation / extracellular matrix structural constituent / Molecules associated with elastic fibres / lung alveolus development / cell adhesion mediated by integrin / cellular response to insulin-like growth factor stimulus / negative regulation of osteoclast differentiation / TGF-beta receptor signaling activates SMADs / basement membrane / anatomical structure morphogenesis / Integrin cell surface interactions / cellular response to transforming growth factor beta stimulus / Degradation of the extracellular matrix / extracellular matrix / skeletal system development / Post-translational protein phosphorylation / hormone activity / integrin binding / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / heparin binding / : / heart development / gene expression / endoplasmic reticulum lumen / calcium ion binding / protein-containing complex binding / extracellular space / extracellular region / identical protein binding
Similarity search - Function
Fibrillin 1, unique N-terminal domain / : / : / Fibrillin 1 unique N-terminal domain / Fibrillin, first EGF domain / TB domain / Extracellular Matrix Fibrillin / TGF-beta binding (TB) domain / TB domain / TGF-beta binding (TB) domain superfamily ...Fibrillin 1, unique N-terminal domain / : / : / Fibrillin 1 unique N-terminal domain / Fibrillin, first EGF domain / TB domain / Extracellular Matrix Fibrillin / TGF-beta binding (TB) domain / TB domain / TGF-beta binding (TB) domain superfamily / TGF-beta binding (TB) domain profile. / EGF domain / EGF domain / Complement Clr-like EGF domain / Complement Clr-like EGF-like / EGF-like, conserved site / Human growth factor-like EGF / : / Calcium-binding EGF domain / Coagulation Factor Xa inhibitory site / EGF-type aspartate/asparagine hydroxylation site / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / Epidermal growth factor-like domain. / EGF-like domain profile. / Growth factor receptor cysteine-rich domain superfamily / EGF-like domain signature 1. / EGF-like domain signature 2. / EGF-like domain / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsYuan, X. / Downing, A.K. / Knott, V. / Handford, P.A.
CitationJournal: EMBO J. / Year: 1997
Title: Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils.
Authors: Yuan, X. / Downing, A.K. / Knott, V. / Handford, P.A.
History
DepositionJul 22, 1997Processing site: BNL
Revision 1.0Jan 28, 1998Provider: 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 / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_ref_seq_dif.details
Revision 1.4Nov 20, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure viewerMolecule:
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Assembly

Deposited unit
A: FIBRILLIN


Theoretical massNumber of molelcules
Total (without water)8,0191
Polymers8,0191
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)21 / -
Representative

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Components

#1: Protein FIBRILLIN


Mass: 8018.965 Da / Num. of mol.: 1
Fragment: TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-LIKE DOMAIN 6(TB6), RESIDUES 2054 - 2125
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Fragment: TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-LIKE DOMAIN 6(TB6), RESIDUES 2054-2125
Plasmid: PQE30 / Production host: Escherichia coli (E. coli) / Strain (production host): NM554 / References: UniProt: P35555
Has protein modificationY

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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
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR softwareName: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 21

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