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- PDB-1gya: N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gya | |||||||||
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Title | N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION DOMAIN OF HUMAN CD2 | |||||||||
![]() | HUMAN CD2 | |||||||||
![]() | ADHESION GLYCOPROTEIN / CELL SURFACE ADHESION RECEPTOR / IMMUNOGLOBULIN SUPERFAMILY V-SET DOMAIN / T LYMPHOCYTE ADHESION GLYCOPROTEIN | |||||||||
Function / homology | ![]() positive regulation of myeloid dendritic cell activation / membrane raft polarization / natural killer cell mediated cytotoxicity / natural killer cell activation / heterotypic cell-cell adhesion / regulation of T cell differentiation / T cell activation / positive regulation of interleukin-8 production / Cell surface interactions at the vascular wall / cytoplasmic side of plasma membrane ...positive regulation of myeloid dendritic cell activation / membrane raft polarization / natural killer cell mediated cytotoxicity / natural killer cell activation / heterotypic cell-cell adhesion / regulation of T cell differentiation / T cell activation / positive regulation of interleukin-8 production / Cell surface interactions at the vascular wall / cytoplasmic side of plasma membrane / receptor tyrosine kinase binding / cell-cell adhesion / : / positive regulation of tumor necrosis factor production / positive regulation of type II interferon production / cell-cell junction / signaling receptor activity / cell surface receptor signaling pathway / external side of plasma membrane / signaling receptor binding / apoptotic process / Golgi apparatus / cell surface / protein-containing complex / extracellular region / nucleoplasm / identical protein binding / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | SOLUTION NMR / distance geometry | |||||||||
![]() | Wyss, D.F. / Choi, J.S. / Wagner, G. | |||||||||
![]() | ![]() Title: Conformation and function of the N-linked glycan in the adhesion domain of human CD2. Authors: Wyss, D.F. / Choi, J.S. / Li, J. / Knoppers, M.H. / Willis, K.J. / Arulanandam, A.R. / Smolyar, A. / Reinherz, E.L. / Wagner, G. #1: ![]() Title: Composition and Sequence Specific Resonance Assignments of the Heterogeneous N-Linked Glycan in the 13.6 KDa Adhesion Domain of Human Cd2 as Determined by NMR on the Intact Glycoprotein Authors: Wyss, D.F. / Choi, J.S. / Wagner, G. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 693.4 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 475.6 KB | Display | ![]() |
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Full document | ![]() | 772.7 KB | Display | |
Data in XML | ![]() | 80.6 KB | Display | |
Data in CIF | ![]() | 96.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 12453.215 Da / Num. of mol.: 1 / Fragment: ADHESION DOMAIN Source method: isolated from a genetically manipulated source Details: GLYCOSYLATED / Source: (gene. exp.) ![]() Description: THE ADHESION DOMAIN OF HUMAN CD2 (HSCD2=105=) WAS OBTAINED BY CLOSTRIPAIN DIGESTION OF THE TWO-DOMAIN HUMAN CD2 (HSCD2=182=) Gene: SCD2=182= / Organ: OVARY / Plasmid: PM1 / Gene (production host): SCD2=182= / Production host: ![]() ![]() |
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#2: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Sample conditions | pH: 4.5 / Temperature: 286 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 | |||||||||
NMR ensemble | Conformer selection criteria: PROSTAT/STRUCT_CHECK / Conformers calculated total number: 120 / Conformers submitted total number: 18 |