1rhp

From Proteopedia

(Difference between revisions)

Revision as of 10:13, 15 September 2021

CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLATELET FACTOR 4

Structural highlights

1rhp is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PLF4_HUMAN] Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form.^[1]

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

The crystal structure of human platelet factor 4 (PF4) has been solved to a resolution of 2.4 A by molecular replacement and refined to an R-factor of 24.1%. The structure consists of four polypeptide chains which form a tetrameric unit. N-terminal residues, previously defined as a random coil or extended loop region, form antiparallel beta-sheet-like structures that form noncovalent associations between dimers. These antiparallel beta-sheet-like structures are positioned lateral to the beta-bilayer motif and stabilize the tetrameric unit. A positively charged ring of lysine and arginine side chains encircles the PF4 tetramer sphere, presenting multiple potential sites and orientations for heparin binding. The electrostatic interactions of multiply charged amino acid side chains and hydrogen bonding interactions at the AB/CD dimer interface serve to stabilize the tetrameric structure further.

Crystal structure of recombinant human platelet factor 4.,Zhang X, Chen L, Bancroft DP, Lai CK, Maione TE Biochemistry. 1994 Jul 12;33(27):8361-6. PMID:8031770^[2]

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

References

↑ Gupta SK, Hassel T, Singh JP. A potent inhibitor of endothelial cell proliferation is generated by proteolytic cleavage of the chemokine platelet factor 4. Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7799-803. PMID:7644496
↑ Zhang X, Chen L, Bancroft DP, Lai CK, Maione TE. Crystal structure of recombinant human platelet factor 4. Biochemistry. 1994 Jul 12;33(27):8361-6. PMID:8031770

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/1rhp"

Categories: Human | Large Structures | Chen, L | Zhang, X | Platelet factor

@@ Line 3: / Line 3: @@
 <StructureSection load='1rhp' size='340' side='right'caption='[[1rhp]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1rhp]] is a 4 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=1RHP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RHP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1rhp]] is a 4 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=1RHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RHP 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=1rhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rhp OCA], [http://pdbe.org/1rhp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rhp RCSB], [http://www.ebi.ac.uk/pdbsum/1rhp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rhp ProSAT]</span></td></tr>
+</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=1rhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rhp OCA], [https://pdbe.org/1rhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rhp RCSB], [https://www.ebi.ac.uk/pdbsum/1rhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rhp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PLF4_HUMAN PLF4_HUMAN]] Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form.<ref>PMID:7644496</ref>
+[[https://www.uniprot.org/uniprot/PLF4_HUMAN PLF4_HUMAN]] Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form.<ref>PMID:7644496</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1rhp

From Proteopedia

Revision as of 10:13, 15 September 2021

CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLATELET FACTOR 4

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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