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| | <StructureSection load='6atv' size='340' side='right'caption='[[6atv]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='6atv' size='340' side='right'caption='[[6atv]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6atv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ATV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ATV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6atv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Orthomyxoviridae Orthomyxoviridae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ATV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ATV FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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]] 1.751Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6atv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6atv OCA], [http://pdbe.org/6atv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6atv RCSB], [http://www.ebi.ac.uk/pdbsum/6atv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6atv ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=6atv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6atv OCA], [https://pdbe.org/6atv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6atv RCSB], [https://www.ebi.ac.uk/pdbsum/6atv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6atv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CRK_HUMAN CRK_HUMAN]] The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.<ref>PMID:1630456</ref> <ref>PMID:11870224</ref> <ref>PMID:17515907</ref> | + | [https://www.uniprot.org/uniprot/CRK_HUMAN CRK_HUMAN] The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.<ref>PMID:1630456</ref> <ref>PMID:11870224</ref> <ref>PMID:17515907</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cho, J H]] | + | [[Category: Orthomyxoviridae]] |
| - | [[Category: Li, P]] | + | [[Category: Cho JH]] |
| - | [[Category: Shen, Q]] | + | [[Category: Li P]] |
| - | [[Category: Zeng, D]] | + | [[Category: Shen Q]] |
| - | [[Category: Zhao, B]] | + | [[Category: Zeng D]] |
| - | [[Category: Crkii]]
| + | [[Category: Zhao B]] |
| - | [[Category: Influenza a virus]]
| + | |
| - | [[Category: Nonstructural protein 1]]
| + | |
| - | [[Category: Protein binding-viral protein complex]]
| + | |
| - | [[Category: Sh3]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
CRK_HUMAN The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.[1] [2] [3]
Publication Abstract from PubMed
Many intrinsically disordered proteins (IDPs) form fuzzy complexes upon binding to their targets. Although many IDPs are weakly bound in fuzzy complexes, some IDPs form high-affinity complexes. One example is the nonstructural protein 1 (NS1) of the 1918 Spanish influenza A virus, which hijacks cellular CRKII through the strong binding affinity (Kd approximately 10 nM) of its proline-rich motif (PRM(NS1)) to the N-terminal Src-homology 3 domain of CRKII. However, its molecular mechanism remains elusive. Here, we examine the interplay between structural disorder of a bound PRM(NS1) and its long-range electrostatic interactions. Using x-ray crystallography and NMR spectroscopy, we found that PRM(NS1) retains substantial conformational flexibility in the bound state. Moreover, molecular dynamics simulations showed that structural disorder of the bound PRM(NS1) increases the number of electrostatic interactions and decreases the mean distances between the positively charged residues in PRM(NS1) and the acidic residues in the N-terminal Src-homology 3 domain. These results are analyzed using a polyelectrostatic model. Our results provide an insight into the molecular recognition mechanism for a high-affinity fuzzy complex.
Molecular Mechanisms of Tight Binding through Fuzzy Interactions.,Shen Q, Shi J, Zeng D, Zhao B, Li P, Hwang W, Cho JH Biophys J. 2018 Mar 27;114(6):1313-1320. doi: 10.1016/j.bpj.2018.01.031. PMID:29590589[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Matsuda M, Tanaka S, Nagata S, Kojima A, Kurata T, Shibuya M. Two species of human CRK cDNA encode proteins with distinct biological activities. Mol Cell Biol. 1992 Aug;12(8):3482-9. PMID:1630456
- ↑ Lawrenson ID, Wimmer-Kleikamp SH, Lock P, Schoenwaelder SM, Down M, Boyd AW, Alewood PF, Lackmann M. Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing 293T and melanoma cells by CrkII and Rho-mediated signalling. J Cell Sci. 2002 Mar 1;115(Pt 5):1059-72. PMID:11870224
- ↑ Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F. Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Nat Struct Mol Biol. 2007 Jun;14(6):503-10. Epub 2007 May 21. PMID:17515907 doi:10.1038/nsmb1241
- ↑ Shen Q, Shi J, Zeng D, Zhao B, Li P, Hwang W, Cho JH. Molecular Mechanisms of Tight Binding through Fuzzy Interactions. Biophys J. 2018 Mar 27;114(6):1313-1320. doi: 10.1016/j.bpj.2018.01.031. PMID:29590589 doi:http://dx.doi.org/10.1016/j.bpj.2018.01.031
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