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[[Image:2py1.gif|left|200px]]<br /><applet load="2py1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2py1" />
'''Solution structure of human liver fatty acid binding protein'''<br />


==Overview==
==Solution structure of human liver fatty acid binding protein==
A new approach is proposed to rapidly determine solution structures of, small and medium-sized 13C,15N-labeled proteins, using a minimal number of, experiments, such as 4D time-shared 13C/15N, 13C/15N-edited NOESY, 3D, HNCA, and 3D MQ-(H)CCH-TOCSY. When the data are recorded on a 500 MHz, spectrometer without using sparse sampling techniques, the experimental, times were minimized to 2.5, 8.5, and 96 h for the HNCA, MQ-(H)CCH-TOCSY, and NOESY, respectively. The time-shared 4D NOESY contains four, sub-spectra, one HC-NOESY-CH, one HC-NOESY-NH, one HN-NOESY-CH, and one, HN-NOESY-NH. Sequence-specific assignment of backbone and side-chain, resonances is achieved from the 3D spectra and the HC-NOESY-NH spectrum., Good initial structures can be quickly calculated using many unambiguous, distance restraints that are easily obtained from the NOESY sub-spectra., The structures can be refined with more restraints assigned based on the, initial structures. The approach has been demonstrated on ubiquitin (76, residues), liver fatty acid binding protein (129 residues, its NMR, assignment and solution structure are presented here for the first time), and a cell-cell adhesion protein (214 residues). The approach will, facilitate high throughput structure determination by NMR.
<StructureSection load='2py1' size='340' side='right'caption='[[2py1]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2py1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PY1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2py1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2py1 OCA], [https://pdbe.org/2py1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2py1 RCSB], [https://www.ebi.ac.uk/pdbsum/2py1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2py1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABPL_HUMAN FABPL_HUMAN] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport.
== 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/py/2py1_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=2py1 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2PY1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PY1 OCA].
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Rapid Data Collection for Protein Structure Determination by NMR Spectroscopy., Xu Y, Long D, Yang D, J Am Chem Soc. 2007 May 31;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17536800 17536800]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Long, D.]]
[[Category: Long D]]
[[Category: Yang, D.]]
[[Category: Yang D]]
[[Category: beta structure]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:29:53 2008''

Latest revision as of 12:44, 22 May 2024

Solution structure of human liver fatty acid binding proteinSolution structure of human liver fatty acid binding protein

Structural highlights

2py1 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABPL_HUMAN Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport.

Evolutionary Conservation

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

See Also

Drag the structure with the mouse to rotate

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OCA
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