User:Karan Hingorani/sandbox 1

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===Functions===
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===Structure===
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DHFR binds everything and is super awesome<scene name='User:Karan_Hingorani/sandbox_1/Dhfr_bound/1'>ooga booga</scene>
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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. <scene name='User:Karan_Hingorani/sandbox_1/Dhfr_bound/1'>ooga booga</scene>

Revision as of 16:23, 14 December 2011

Contents

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.


Catalysis

Test

E.coli Apo-DHFR

Drag the structure with the mouse to rotate
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

Proteopedia Page Contributors and Editors (what is this?)

Karan Hingorani

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