1hmr

From Proteopedia

(Difference between revisions)

Current revision

1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDING PROTEIN: BINDING INTERACTIONS WITH THREE SATURATED AND UNSATURATED C18 FATTY ACIDS

Structural highlights

1hmr is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.4Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABPH_HUMAN FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.

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 PubMed

BACKGROUND: Muscle fatty acid binding protein (M-FABP) is one of a family of cytosolic lipid-binding proteins involved in fatty acid processing. In order to investigate the precise interactions between M-FABP and its ligands and to understand the structural basis of differential binding affinity, we have compared the structures of M-FABP in complex with three C18 fatty acids. RESULTS: We describe the crystal structures of M-FABP in complex with n-octadecanoate (stearate), trans-delta 9-octadecenoate (elaidate) and cis-delta 9-octadecenoate (oleate). These structures were refined using least-squares positional and anisotropic temperature factor refinement to final R-factors of 11.4%, 12.1% and 13.2% respectively for all the data between 8.0 A and 1.4 A resolution. CONCLUSIONS: Stearate, elaidate and oleate each adopt highly similar U-shaped conformations when they bind to M-FABP within a large interior binding cavity, which also contains 13 ordered water molecules. The atomic structure of the protein is virtually identical, regardless of the nature of the bound ligand. The fatty acid is thought to enter the interior cavity of the protein via a portal in its surface while interior solvent is released through a secondary opening. The ligand affinity can be correlated with the conformational energy and the solubility of the bound ligand.

Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids.,Young AC, Scapin G, Kromminga A, Patel SB, Veerkamp JH, Sacchettini JC Structure. 1994 Jun 15;2(6):523-34. PMID:7922029^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Young AC, Scapin G, Kromminga A, Patel SB, Veerkamp JH, Sacchettini JC. Structural studies on human muscle fatty acid binding protein at 1.4 A resolution: binding interactions with three C18 fatty acids. Structure. 1994 Jun 15;2(6):523-34. PMID:7922029

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hmr"

@@ Line 1: / Line 1: @@
 ==1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDING PROTEIN: BINDING INTERACTIONS WITH THREE SATURATED AND UNSATURATED C18 FATTY ACIDS==
-<StructureSection load='1hmr' size='340' side='right' caption='[[1hmr]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+<StructureSection load='1hmr' size='340' side='right'caption='[[1hmr]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1hmr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HMR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1hmr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HMR FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ELA:9-OCTADECENOIC+ACID'>ELA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmr OCA], [http://pdbe.org/1hmr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hmr RCSB], [http://www.ebi.ac.uk/pdbsum/1hmr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmr ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ELA:9-OCTADECENOIC+ACID'>ELA</scene></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=1hmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmr OCA], [https://pdbe.org/1hmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hmr RCSB], [https://www.ebi.ac.uk/pdbsum/1hmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FABPH_HUMAN FABPH_HUMAN]] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
+[https://www.uniprot.org/uniprot/FABPH_HUMAN FABPH_HUMAN] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
 == 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/hm/1hmr_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/1hmr_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1hmr" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Kromminga, A]]
+[[Category: Large Structures]]
-[[Category: Patel, S B]]
+[[Category: Kromminga A]]
-[[Category: Sacchettini, J C]]
+[[Category: Patel SB]]
-[[Category: Scapin, G]]
+[[Category: Sacchettini JC]]
-[[Category: Veerkamp, J H]]
+[[Category: Scapin G]]
-[[Category: Young, A C.M]]
+[[Category: Veerkamp JH]]
-[[Category: Lipid binding protein]]
+[[Category: Young ACM]]
-[[Category: Lipid-binding protein]]

1hmr

From Proteopedia

Current revision

1.4 ANGSTROMS STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID BINDING PROTEIN: BINDING INTERACTIONS WITH THREE SATURATED AND UNSATURATED C18 FATTY ACIDS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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