6BYV

Solution NMR structure of cysteine-rich calcium bound domains of very low density lipoprotein receptor

Summary for 6BYV

• Entry DOI: 10.2210/pdb6byv/pdb
• NMR Information: BMRB: 30388
• Descriptor: Very low-density lipoprotein receptor, CALCIUM ION (2 entities in total)
• Functional Keywords: 3 modules, calcium-bound domains, disulfide bonds, structural protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 13295.33

Authors

Banerjee, K.,Gruschus, J.M.,Tjandra, N.,Yakovlev, S.,Medved, L. (deposition date: 2017-12-21, release date: 2018-07-18, Last modification date: 2024-11-20)

Primary citation

Banerjee, K.,Yakovlev, S.,Gruschus, J.M.,Medved, L.,Tjandra, N.
Nuclear Magnetic Resonance Solution Structure of the Recombinant Fragment Containing Three Fibrin-Binding Cysteine-Rich Domains of the Very Low Density Lipoprotein Receptor.
Biochemistry, 57:4395-4403, 2018

PubMed Abstract: Our previous studies revealed that interaction of fibrin with the very low density lipoprotein (VLDL) receptor plays a prominent role in transendothelial migration of leukocytes and thereby inflammation. The major goal of our subsequent studies is to establish the structural basis for this interaction. As the first step toward this goal, we localized the fibrin-binding sites within cysteine-rich (CR) domains 2-4 of the VLDL receptor. In this study, we have made a next step toward this goal by establishing the nuclear magnetic resonance solution structure of the recombinant VLDLR(2-4) fragment containing all three fibrin-binding CR domains of this receptor. The structure revealed that all three CR domains have a similar general fold. Each domain contains a calcium-binding loop, and the loop in the CR3 domain has a unique conformation relative to the other two. Domains CR2 and CR3 interact with each other, while CR4 is flexible relative to the other two domains. In addition, analysis of the electrostatic potential surface of VLDLR(2-4) revealed extended negatively charged regions in each of its CR domains. The presence of these regions suggests that they may interact with three positively charged clusters of the fibrin βN domain whose involvement in interaction with the VLDL receptor was demonstrated earlier. Altogether, these findings provide a solid background for our next step toward establishing the structural basis for fibrin-VLDL receptor interaction.

PubMed: 29965730
DOI: 10.1021/acs.biochem.8b00349

Experimental method

SOLUTION NMR