4wmu

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STRUCTURE OF MBP-MCL1 BOUND TO ligand 2 AT 1.55A

Structural highlights

4wmu is a 1 chain structure with sequence from Escherichia coli K-12 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.55Å
Ligands:19H, EDO, FMT, GLC, MG, NA, PRD_900001
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.MCL1_HUMAN Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis.[1]

Publication Abstract from PubMed

Crystallization of a maltose-binding protein MCL1 fusion has yielded a robust crystallography platform that generated the first apo MCL1 crystal structure, as well as five ligand-bound structures. The ability to obtain fragment-bound structures advances structure-based drug design efforts that, despite considerable effort, had previously been intractable by crystallography. In the ligand-independent crystal form we identify inhibitor binding modes not observed in earlier crystallographic systems. This MBP-MCL1 construct dramatically improves the structural understanding of well-validated MCL1 ligands, and will likely catalyze the structure-based optimization of high affinity MCL1 inhibitors.

A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1.,Clifton MC, Dranow DM, Leed A, Fulroth B, Fairman JW, Abendroth J, Atkins KA, Wallace E, Fan D, Xu G, Ni ZJ, Daniels D, Van Drie J, Wei G, Burgin AB, Golub TR, Hubbard BK, Serrano-Wu MH PLoS One. 2015 Apr 24;10(4):e0125010. doi: 10.1371/journal.pone.0125010., eCollection 2015. PMID:25909780[2]

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

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See Also

References

  1. ↑ Bingle CD, Craig RW, Swales BM, Singleton V, Zhou P, Whyte MK. Exon skipping in Mcl-1 results in a bcl-2 homology domain 3 only gene product that promotes cell death. J Biol Chem. 2000 Jul 21;275(29):22136-46. PMID:10766760 doi:10.1074/jbc.M909572199
  2. ↑ Clifton MC, Dranow DM, Leed A, Fulroth B, Fairman JW, Abendroth J, Atkins KA, Wallace E, Fan D, Xu G, Ni ZJ, Daniels D, Van Drie J, Wei G, Burgin AB, Golub TR, Hubbard BK, Serrano-Wu MH. A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1. PLoS One. 2015 Apr 24;10(4):e0125010. doi: 10.1371/journal.pone.0125010., eCollection 2015. PMID:25909780 doi:http://dx.doi.org/10.1371/journal.pone.0125010

Contents


PDB ID 4wmu

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OCA

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