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3zfw

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Revision as of 11:33, 25 December 2014

Crystal structure of the TPR domain of kinesin light chain 2 in complex with a tryptophan-acidic cargo peptide

Structural highlights

3zfw is a 4 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PKHM2_HUMAN] May play a role in the regulation of conventional kinesin activity. Required for maintenance of the Golgi apparatus organization. May play a role in membrane tubulation.^[1]

Publication Abstract from PubMed

Kinesin-mediated cargo transport is required for many cellular functions and plays a key role in pathological processes. Structural information on how kinesins recognize their cargoes is required for a molecular understanding of this fundamental and ubiquitous process. Here, we present the crystal structure of the tetratricopeptide repeat of kinesin light chain 2 in complex with a cargo peptide harboring a 'tryptophan-acidic' motif derived from SKIP, a critical host determinant in Salmonella pathogenesis and a regulator of lysosomal positioning. Structural data together with biophysical, biochemical, and cellular assays allow us to propose a framework for intracellular transport based on the binding by kinesin-1 of W-acidic cargo motifs through a combination of electrostatic interactions and sequence-specific elements, providing direct molecular evidence of the mechanisms for kinesin-1:cargo recognition.

Structural Basis For Kinesin-1:Cargo Recognition.,Pernigo S, Lamprecht A, Steiner RA, Dodding MP Science. 2013 Mar 21. PMID:23519214^[2]

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

References

↑ Boucrot E, Henry T, Borg JP, Gorvel JP, Meresse S. The intracellular fate of Salmonella depends on the recruitment of kinesin. Science. 2005 May 20;308(5725):1174-8. PMID:15905402 doi:308/5725/1174
↑ Pernigo S, Lamprecht A, Steiner RA, Dodding MP. Structural Basis For Kinesin-1:Cargo Recognition. Science. 2013 Mar 21. PMID:23519214 doi:http://dx.doi.org/10.1126/science.1234264

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3zfw"

@@ Line 5: / Line 5: @@
 </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=3zfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zfw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zfw RCSB], [http://www.ebi.ac.uk/pdbsum/3zfw PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PKHM2_HUMAN PKHM2_HUMAN]] May play a role in the regulation of conventional kinesin activity. Required for maintenance of the Golgi apparatus organization. May play a role in membrane tubulation.<ref>PMID:15905402</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3zfw

From Proteopedia

Revision as of 11:33, 25 December 2014

Crystal structure of the TPR domain of kinesin light chain 2 in complex with a tryptophan-acidic cargo peptide

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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