1rhg

<table><tr><td colspan='2'>[[1rhg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RHG FirstGlance]. <br>

</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=1rhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rhg OCA], [https://pdbe.org/1rhg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rhg RCSB], [https://www.ebi.ac.uk/pdbsum/1rhg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rhg ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/CSF3_HUMAN CSF3_HUMAN]] Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.

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== Publication Abstract from PubMed ==

We have determined the three-dimensional structure of recombinant human granulocyte-colony-stimulating factor by x-ray crystallography. Phases were initially obtained at 3.0-A resolution by multiple isomorphous replacement and were refined by solvent flattening and by averaging of the electron density of the three molecules in the asymmetric unit. The current R factor is 21.5% for all data between 6.0- and 2.2-A resolution. The structure is predominantly helical, with 104 of the 175 residues forming a four-alpha-helix bundle. The only other secondary structure is also helical. In the loop between the first two long helices a four-residue 3(10)-helix is immediately followed by a 6-residue alpha-helix. Three residues in the short connection between the second and third bundle helices form almost one turn of left-handed helix. The up-up-down-down connectivity with two long crossover connections has been reported previously for five other proteins, which like granulocyte-colony-stimulating factor are all signaling ligands: growth hormone, granulocyte/macrophage-colony-stimulating factor, interferon beta, interleukin 2, and interleukin 4. Structural similarity among these growth factors occurs despite the absence of similarity in their amino acid sequences. Conservation of this tertiary structure suggests that these different growth factors might all bind to their respective sequence-related receptors in an equivalent manner.

The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors.,Hill CP, Osslund TD, Eisenberg D Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5167-71. PMID:7685117<ref>PMID:7685117</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Human]]

[[Category: Eisenberg, D]]

[[Category: Hill, C P]]

[[Category: Osslund, T D]]

[[Category: Growth factor]]