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- SASDB76: Deglycosylated myelin-associated glycoprotein (immunoglobulin dom... -
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Open data
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Basic information
Entry | Database: SASBDB / ID: SASDB76 |
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![]() | Deglycosylated myelin-associated glycoprotein (immunoglobulin domains 1-3)
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Function / homology | ![]() mesaxon / Axonal growth inhibition (RHOA activation) / Basigin interactions / ganglioside GT1b binding / sialic acid binding / central nervous system myelination / positive regulation of myelination / myelin sheath adaxonal region / central nervous system myelin formation / negative regulation of axon extension ...mesaxon / Axonal growth inhibition (RHOA activation) / Basigin interactions / ganglioside GT1b binding / sialic acid binding / central nervous system myelination / positive regulation of myelination / myelin sheath adaxonal region / central nervous system myelin formation / negative regulation of axon extension / cell-cell adhesion via plasma-membrane adhesion molecules / paranode region of axon / Schmidt-Lanterman incisure / positive regulation of astrocyte differentiation / axon regeneration / transmission of nerve impulse / negative regulation of neuron differentiation / myelination / cellular response to mechanical stimulus / negative regulation of neuron projection development / myelin sheath / carbohydrate binding / negative regulation of neuron apoptotic process / cell adhesion / membrane raft / signaling receptor binding / protein kinase binding / protein homodimerization activity / plasma membrane Similarity search - Function |
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![]() | ![]() Title: Structural basis of myelin-associated glycoprotein adhesion and signalling. Authors: Matti F Pronker / Suzanne Lemstra / Joost Snijder / Albert J R Heck / Dominique M E Thies-Weesie / R Jeroen Pasterkamp / Bert J C Janssen / ![]() Abstract: Myelin-associated glycoprotein (MAG) is a myelin-expressed cell-adhesion and bi-directional signalling molecule. MAG maintains the myelin-axon spacing by interacting with specific neuronal ...Myelin-associated glycoprotein (MAG) is a myelin-expressed cell-adhesion and bi-directional signalling molecule. MAG maintains the myelin-axon spacing by interacting with specific neuronal glycolipids (gangliosides), inhibits axon regeneration and controls myelin formation. The mechanisms underlying MAG adhesion and signalling are unresolved. We present crystal structures of the MAG full ectodomain, which reveal an extended conformation of five Ig domains and a homodimeric arrangement involving membrane-proximal domains Ig4 and Ig5. MAG-oligosaccharide complex structures and biophysical assays show how MAG engages axonal gangliosides at domain Ig1. Two post-translational modifications were identified-N-linked glycosylation at the dimerization interface and tryptophan C-mannosylation proximal to the ganglioside binding site-that appear to have regulatory functions. Structure-guided mutations and neurite outgrowth assays demonstrate MAG dimerization and carbohydrate recognition are essential for its regeneration-inhibiting properties. The combination of trans ganglioside binding and cis homodimerization explains how MAG maintains the myelin-axon spacing and provides a mechanism for MAG-mediated bi-directional signalling. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
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External links
Related items in Molecule of the Month |
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-Models
Model #584 | ![]() Type: atomic / Software: Crysol (2.8.3) / Radius of dummy atoms: 1.90 A Comment: Glycans were trimmed off the model to match the SAXS curve of the deglycosylated sample Chi-square value: 3.845521 ![]() |
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Sample
![]() | Name: Deglycosylated myelin-associated glycoprotein (immunoglobulin domains 1-3) Specimen concentration: 1.39 mg/ml |
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Buffer | Name: HEPES / Concentration: 20.00 mM / pH: 7.5 / Composition: 150 mM NaCl |
Entity #396 | Name: MAG / Type: protein / Description: Myelin-associated glycoprotein Ig domains 1-3 / Formula weight: 34.98 / Num. of mol.: 1 / Source: Mus musculus / References: UniProt: P20917 Sequence: GSGHWGAWMP STISAFEGTC VSIPCRFDFP DELRPAVVHG VWYFNSPYPK NYPPVVFKSR TQVVHESFQG RSRLLGDLGL RNCTLLLSTL SPELGGKYYF RGDLGGYNQY TFSEHSVLDI VNTPNIVVPP EVVAGTEVEV SCMVPDNCPE LRPELSWLGH EGLGEPTVLG ...Sequence: GSGHWGAWMP STISAFEGTC VSIPCRFDFP DELRPAVVHG VWYFNSPYPK NYPPVVFKSR TQVVHESFQG RSRLLGDLGL RNCTLLLSTL SPELGGKYYF RGDLGGYNQY TFSEHSVLDI VNTPNIVVPP EVVAGTEVEV SCMVPDNCPE LRPELSWLGH EGLGEPTVLG RLREDEGTWV QVSLLHFVPT REANGHRLGC QAAFPNTTLQ FEGYASLDVK YPPVIVEMNS SVEAIEGSHV SLLCGADSNP PPLLTWMRDG MVLREAVAKS LYLDLEEVTP GEDGVYACLA ENAYGQDNRT VELSVMYAAA AHHHHHH |
-Experimental information
Beam | Instrument name: ESRF BM29 / City: Grenoble / 国: France ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M | ||||||||||||||||||||||||||||||
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Distance distribution function P(R) |
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Result | Comments: Endo-Hf-deglycosylated Myelin-associated glycoprotein (MAG) immunoglobulin domains 1-3
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