Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 1998 May 4;141(3):553–566. doi: 10.1083/jcb.141.3.553

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

PMC Copyright notice

Amino acid sequence analysis of NRP/B. (A) Deduced amino acid sequence of NRP/B. The BTB/ POZ homologous domain is underlined. (B) Sequence alignment of the 50–amino acid β-sheet repetitive domains. Sequence alignment indicates the 50–amino acid putative β-sheet repetitive domains compared with the most related protein, Drosophila kelch (d), with 28% identity (45% similarity). The consensus is indicated on the top line: capital letters, highly conserved residues; underlined italics, hydrophobic residues; #, hydrophilic residues; *, charged residues. Letters in shaded boxes denote hydrophobic or charged residues. White letters on black background represent conserved residues. Dashes indicate gaps in the alignment. The three digit numbers in the left column indicate the number of the first residue (or amino acid) in each repeat, and the numbers in the right column indicate the number of residues in a repeat.