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I agree with Ruud.  That is a typical amphipathic helical arrangement.

Cheers,

Chris

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Christopher L. Colbert, Ph.D.

Associate Professor

Department of Chemistry and Biochemistry

North Dakota State University

P.O. Box 6050 Dept. 2710

Fargo, ND 58108-6050

PH: (701) 231-7946

FAX: (701) 231-8324

From: CCP4 bulletin board <[log in to unmask]> on behalf of Ruud Hovius <[log in to unmask]>
Reply-To: Ruud Hovius <[log in to unmask]>
Date: Saturday, March 3, 2018 at 5:50 PM
To: "[log in to unmask]" <[log in to unmask]>
Subject: Re: [ccp4bb] A helix with leucine repeats

an amphiphatic helix ? if so a classical motif of membrane binding peptides

Best greetings, Ruud

On 3/3/18 21:51, Cheng Zhang wrote:
[log in to unmask]">
Hi all,

We recently got a structure of a transmembrane protein. There is a helix that is parallel to the membrane. The function of this helix is not known and we are trying to make some hypothesis. A unique feature is that there are repeated leucine residues on this helix facing the lipids. I am wondering if anyone has seen a similar pattern and could suggest possible function, e.g. membrane anchoring?

Thanks!

Best,

Cheng




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Cheng Zhang

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Ruud Hovius
EPFL SB ISIC LCBM 
Office CH B3 424
CH-1015 Lausanne
+41-21-693-3134
http://people.epfl.ch/ruud.hovius