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Contents 1 Introduction 2 Structure 3 Catalysis 4 Drug Target 5 PDB structures 6 References

Introduction

Dihydrofolate Reductase (DHFR) is a crucial metabolic enzyme whose function is to reduce Dihydrofolate to Tetrahydrofolate, which can then be incorporated into the synthesis of Purines and amino acids. DHFR is classified as an oxidoreductase, which uses NADP+ as the electron acceptor (EC: 1.5.1.3). It is ubiquitously found and is now a popular target for anticancer drugs and antibiotics. free of any of its ligands is displayed here.

Structure

E.coli DHFR is a small 159 amino acid protein approximately 18kDa. It has an a/b structure with eight central B strands and four helices. The protein can be thought to be made up of two subdomains, divided by the active site cleft. The which consists of residues 38-88 and the major subdomain comprised of about 100 residues. Three loops can be found in the major subdomain and they make up about 50% of this domain. They are the (residues 9-24, the (residues 116-132)and the (residues 142-150). The Met20 loop assumes different conformations during catalysis and accomodation of ligands is made possible by the 'hinge bending' motion about Lys 38 and Val 88 of the Adenosine binding domain.

Catalysis

Test

spinqualitylabelsall models E.coli Apo-DHFR Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

DHFR is an enzyme that does blah blah. === Ligand-binding domain ===

Drug Target

metho and trimetho [1].

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PDB structures

2cbr - hCRABP I – human
1cbr - CRABP I + retinoic acid – mouse

References