1ihc: Difference between revisions

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[[Image:1ihc.png|left|200px]]


{{STRUCTURE_1ihc| PDB=1ihc | SCENE= }}
==X-ray Structure of Gephyrin N-terminal Domain==
<StructureSection load='1ihc' size='340' side='right'caption='[[1ihc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ihc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IHC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ihc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ihc OCA], [https://pdbe.org/1ihc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ihc RCSB], [https://www.ebi.ac.uk/pdbsum/1ihc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ihc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GEPH_RAT GEPH_RAT] Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.<ref>PMID:8264797</ref> <ref>PMID:9990024</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ih/1ihc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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=1ihc ConSurf].
<div style="clear:both"></div>


===X-ray Structure of Gephyrin N-terminal Domain===
==See Also==
 
*[[Gephyrin|Gephyrin]]
{{ABSTRACT_PUBMED_11325967}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1ihc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IHC OCA].
</StructureSection>
 
[[Category: Large Structures]]
==Reference==
<ref group="xtra">PMID:011325967</ref><references group="xtra"/>
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Betz, H.]]
[[Category: Betz H]]
[[Category: Heck, I S.]]
[[Category: Heck IS]]
[[Category: Kneussel, M.]]
[[Category: Kneussel M]]
[[Category: Sola, M.]]
[[Category: Sola M]]
[[Category: Weissenhorn, W.]]
[[Category: Weissenhorn W]]
[[Category: Alpha/beta]]
[[Category: Contractile protein]]

Latest revision as of 10:35, 7 February 2024

X-ray Structure of Gephyrin N-terminal DomainX-ray Structure of Gephyrin N-terminal Domain

Structural highlights

1ihc is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GEPH_RAT Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Kirsch J, Wolters I, Triller A, Betz H. Gephyrin antisense oligonucleotides prevent glycine receptor clustering in spinal neurons. Nature. 1993 Dec 23-30;366(6457):745-8. PMID:8264797 doi:http://dx.doi.org/10.1038/366745a0
  2. Stallmeyer B, Schwarz G, Schulze J, Nerlich A, Reiss J, Kirsch J, Mendel RR. The neurotransmitter receptor-anchoring protein gephyrin reconstitutes molybdenum cofactor biosynthesis in bacteria, plants, and mammalian cells. Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1333-8. PMID:9990024

1ihc, resolution 1.90Å

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