1agq: Difference between revisions
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ag/1agq_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ag/1agq_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1agq ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1agq ConSurf]. | ||
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== Publication Abstract from PubMed == | |||
The crystal structure of glial cell-derived neurotrophic factor (GDNF) reveals two independent copies of the dimer that differ significantly through a hinge bending at the central, disulphide-rich region. GDNF is compared with other members of the TGF-beta family, and potential receptor binding surfaces are identified. | |||
X-ray structure of glial cell-derived neurotrophic factor at 1.9 A resolution and implications for receptor binding.,Eigenbrot C, Gerber N Nat Struct Biol. 1997 Jun;4(6):435-8. PMID:9187648<ref>PMID:9187648</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 1agq" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 02:47, 21 November 2024
GLIAL CELL-DERIVED NEUROTROPHIC FACTOR FROM RATGLIAL CELL-DERIVED NEUROTROPHIC FACTOR FROM RAT
Structural highlights
FunctionGDNF_RAT Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake. May also modulate local neuronal effects in distal regions of the motor neuron.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of glial cell-derived neurotrophic factor (GDNF) reveals two independent copies of the dimer that differ significantly through a hinge bending at the central, disulphide-rich region. GDNF is compared with other members of the TGF-beta family, and potential receptor binding surfaces are identified. X-ray structure of glial cell-derived neurotrophic factor at 1.9 A resolution and implications for receptor binding.,Eigenbrot C, Gerber N Nat Struct Biol. 1997 Jun;4(6):435-8. PMID:9187648[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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