2gmf: Difference between revisions
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<StructureSection load='2gmf' size='340' side='right' caption='[[2gmf]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2gmf' size='340' side='right' caption='[[2gmf]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2gmf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2gmf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1gmf 1gmf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GMF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GMF FirstGlance]. <br> | ||
</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=2gmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gmf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gmf RCSB], [http://www.ebi.ac.uk/pdbsum/2gmf PDBsum]</span></td></tr> | </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=2gmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gmf OCA], [http://pdbe.org/2gmf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gmf RCSB], [http://www.ebi.ac.uk/pdbsum/2gmf PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2gmf" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Human]] | ||
[[Category: Boone, T]] | [[Category: Boone, T]] | ||
[[Category: Diederichs, K]] | [[Category: Diederichs, K]] | ||
Revision as of 15:17, 11 September 2015
HUMAN GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTORHUMAN GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR
Structural highlights
Function[CSF2_HUMAN] Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. 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 recombinant human granulocyte-macrophage colony stimulating factor (rhGM-CSF) has been refined against data extending to a resolution of approximately 2.4 A along a* and approximately 1.9 A along b* and c*. Anisotropic scale factors of B11 = -20.8 A2, B22 = 7.4 A2, B33 = 13.3 A2 corrected for the more rapid fall of diffraction in the a* direction. The anisotropy correlates with the weak crystal packing interactions along the a axis. In addition to apolar side chains in the protein core, there are 10 buried hydrogen bonding residues. Those residues involved in intramolecular hydrogen bonding to main chain atoms are better conserved than those hydrogen bonding to other side chain atoms; 24 solvation sites are observed at equivalent positions in the two molecules in the asymmetric unit, and the strongest among these are located in clefts between secondary structural elements. No buried water sites are seen. Two surface clusters of hydrophobic side chains are located near the expected receptor binding regions. Mutagenesis of 11 residues on the helix A/helix C face confirms the importance of Glu-21 and shows that Gly-75 and Gln-86, located on helix C, each cause a greater than fourfold drop in activity. Glu-21 and Gly-75, but not Gln-86, are structurally equivalent to residues involved in the growth hormone binding to its receptor. Refined crystal structure and mutagenesis of human granulocyte-macrophage colony-stimulating factor.,Rozwarski DA, Diederichs K, Hecht R, Boone T, Karplus PA Proteins. 1996 Nov;26(3):304-13. PMID:8953651[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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